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Book: Elämän pakkoraossa vai matkalla vaurauteen

Kettunen-Hujanen, Eija

Savosta, Pohjois-Karjalasta ja Kainuusta 1918 - 1930 muuttaneiden siirtolaisten sopeutuminen Kanadaan

(Bibliotheca historica ; 58)

2000

Author's details	Eija Kettunen-Hujanen
Series title	Bibliotheca historica ; 58
Language	Finnish
Size	235 p
Publisher	Suomalaisen Kirjallisuuden Seura
Publishing place	Helsinki
Document type	Book
Note	Zsfassung in engl. Sprache
ISBN	9517461887 ; 9789517461887
Database	Former special subject collection: coastal and deep sea fishing

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Article: Fibroblasts stimulate human ovarian cancer cell invasion and expression of 72-kDa gelatinase A (MMP-2).

Westerlund, A / Hujanen, E / Puistola, U / Turpeenniemi-Hujanen, T

Gynecologic oncology

1997 Volume 67, Issue 1, Page(s) 76–82

Abstract: Objective: The host-tumor interactions and tumor stroma may participate in the regulation of invasive behavior of tumor cells. In order to better understand the human ovarian cancer invasion we explored the possibility that normal fibroblasts could ... ...

Abstract	Objective: The host-tumor interactions and tumor stroma may participate in the regulation of invasive behavior of tumor cells. In order to better understand the human ovarian cancer invasion we explored the possibility that normal fibroblasts could participate in the control of the spread of human ovarian cancer. Results: A 3.5-fold increase (from 2.83 +/- 0.97 to 10.2 +/- 3.43%) in human ovarian cancer cell (Ovcar-3) invasion through a reconstituted basement membrane was noted when normal fibroblasts (CRL 1295) were added to the invasion chambers in conjunction with tumor cells. Conditioned medium from either fibroblasts or Ovcar-3 also enhanced the in vitro invasion of Ovcar-3 by 2- to 2.5-fold (from 2.83 +/- 0.97 to 5.71 +/- 3.5 and to 7.15 +/- 1.2%, respectively) compared to nonstimulated control cells. Zymographic analysis and assays of mRNA for the 72-kDa matrix metalloproteinase (MMP-2) showed that Ovcar-3 cells alone produced very low levels of MMP-2; the expression of this gelatinase was detectable in zymography only with stimulation by incubation of these cells with conditioned media from either fibroblasts or ovarian cancer cells themselves. Interestingly, MMP-2 activity was increased also in fibroblasts when using either ovarian cancer cell-conditioned (to 178 +/- 67%) or fibroblast-conditioned medium (to 215 +/- 61%) and the gene expression for MMP-2 was similarly increased in both fibroblasts and Ovcar-3 cells when using either fibroblast-conditioned medium or ovarian cancer cell-conditioned medium from 1.00 +/- 0.25 to 2.20 +/- 0.50 and 1.86 +/- 0.10 in fibroblasts and from 1.00 +/- 0.26 to 1.60 +/- 0.34 and 2.15 +/- 0.30 in Ovcar-3 cells, respectively. Conclusions: These results show that interplay between tumor cells and normal cells in the control of invasion and secretion of proteolytic enzymes may involve not only paracrine but also autocrine elements. Thus, such interactions are possible and may play an important role in the spread of cancer.
MeSH term(s)	Cell Communication/physiology ; Culture Media, Conditioned ; Female ; Fibroblasts/cytology ; Gelatinases/metabolism ; Humans ; Matrix Metalloproteinase 2 ; Metalloendopeptidases/metabolism ; Molecular Weight ; Neoplasm Invasiveness ; Ovarian Neoplasms/enzymology ; Ovarian Neoplasms/pathology
Chemical Substances	Culture Media, Conditioned ; Gelatinases (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-) ; Matrix Metalloproteinase 2 (EC 3.4.24.24)
Language	English
Publishing date	1997-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	801461-9
ISSN	1095-6859 ; 0090-8258
ISSN (online)	1095-6859
ISSN	0090-8258
DOI	10.1006/gyno.1997.4808
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Article: A laminin graft replaces neurorrhaphy in the restorative surgery of the rat sciatic nerve.

Kauppila, T / Jyväsjärvi, E / Huopaniemi, T / Hujanen, E / Liesi, P

Experimental neurology

1993 Volume 123, Issue 2, Page(s) 181–191

Abstract: We investigated the role of laminin in functional recovery of a peripheral nerve injury using electrophysiological and behavioral approaches on the rat sciatic nerve in vivo. These studies were complemented by neurofilament protein immunocytochemistry on ...

Abstract	We investigated the role of laminin in functional recovery of a peripheral nerve injury using electrophysiological and behavioral approaches on the rat sciatic nerve in vivo. These studies were complemented by neurofilament protein immunocytochemistry on the sciatic nerve 20 days after an operation, in which an 8-mm piece of the nerve was removed and replaced by a graft of laminin, its neurite outgrowth-promoting peptide, a control peptide, collagen, or by resuturing of the removed piece of the nerve. Electrophysiological measurements of muscle strength 4 months after the sciatic nerve transection showed that a laminin graft was as effective as neurorrhaphy in supporting functional recovery of an injured peripheral nerve. A laminin graft also significantly reduced autotomy in the operated animals. Immunocytochemistry confirmed that both a laminin graft and resuturing supported growth of the 200-kDa neurofilament-positive axons into the distal stump of the nerve within 20 days of operation. A graft with a neurite outgrowth-promoting peptide of the B2 chain of laminin supported similar axon growth, whereas another peptide graft also derived from laminin or a collagen graft did not support axon growth. All grafts allowed Schwann cell growth into the distal stumps of the nerves, but neurites accompanied them only in the regeneration-supporting grafts and in the resutured nerves. The Schwann cells of the regenerating nerves expressed high levels of the neurite outgrowth-promoting domain of the B2 chain of laminin, whereas the Schwann cells of the degenerating nerves failed to express this domain in the distal stumps of the degenerating nerves. These results provide the first in vivo evidence for the functional role of laminin in peripheral nerve regeneration. As the neurite outgrowth-promoting domain of the B2 chain of laminin is as efficient as laminin or resuturing in supporting a short-term recovery of an injured sciatic nerve, this area may be a regeneration-promoting domain of this glycoprotein. More importantly, as grafting significantly reduces post-traumatic pain behavior in the operated animals, the laminin graft surgery may provide a useful method for clinical restoration of the injured peripheral nerves.
MeSH term(s)	Animals ; Axons/physiology ; Behavior, Animal ; Electrophysiology ; Female ; Laminin/physiology ; Muscles/innervation ; Muscles/physiology ; Nerve Regeneration ; Neurites/physiology ; Neurofilament Proteins/chemistry ; Rats ; Rats, Wistar ; Receptors, Nerve Growth Factor/metabolism ; Schwann Cells/physiology ; Sciatic Nerve/metabolism ; Sciatic Nerve/physiology
Chemical Substances	Laminin ; Neurofilament Proteins ; Receptors, Nerve Growth Factor
Language	English
Publishing date	1993-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	207148-4
ISSN	1090-2430 ; 0014-4886
ISSN (online)	1090-2430
ISSN	0014-4886
DOI	10.1006/exnr.1993.1151
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Article: 70 K type IV collagenase (gelatinase).

Tryggvason, K / Huhtala, P / Höyhtya, M / Hujanen, E / Hurskainen, T

Matrix (Stuttgart, Germany). Supplement

1992 Volume 1, Page(s) 45–50

Abstract: Type IV collagenase (gelatinase) is a 70,000 dalton neutral metalloproteinase that specifically cleaves type IV collagen in addition to degrading denatured collagen (gelatin). It is secreted in a latent proenzyme form that is converted proteolytically in ...

Abstract	Type IV collagenase (gelatinase) is a 70,000 dalton neutral metalloproteinase that specifically cleaves type IV collagen in addition to degrading denatured collagen (gelatin). It is secreted in a latent proenzyme form that is converted proteolytically in the extracellular space to a 62,000 dalton active enzyme. The primary structure, enzymatic properties as well as gene structure, demonstrate that type IV collagenase is closely related with the other well characterized metalloproteinases, interstitial collagenase and stromelysin. However, the structure of type IV collagenase differs from the others in that it is larger and contains three internal repeats that resemble the type II domains of fibronectin. Also, initial characterization of the promoter region of the gene indicates that its regulation differs from the other proteinase genes. Type IV collagenase is presumably required for the normal turnover of basement membranes. Augmented activity is linked with the invasive potential of tumor cells and the enzyme is believed to play a major role in the penetration of basement membranes by metastatic cells. Measurements of enzyme activity and mRNA levels as well as immunostaining of a variety of tumor cells and tissues suggest that assays for the enzyme may have value in the follow-up of malignant growth.
MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Basement Membrane/metabolism ; Collagenases/chemistry ; Collagenases/genetics ; Collagenases/immunology ; Collagenases/physiology ; Genes ; Humans ; Matrix Metalloproteinase 9 ; Molecular Sequence Data ; Molecular Weight ; Neoplasm Invasiveness ; Neoplasm Proteins/physiology ; Rabbits ; Rats ; Sequence Alignment ; Substrate Specificity
Chemical Substances	Neoplasm Proteins ; Collagenases (EC 3.4.24.-) ; Matrix Metalloproteinase 9 (EC 3.4.24.35)
Language	English
Publishing date	1992
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	0940-1199
ISSN	0940-1199
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Article: Ovarian cancer cell invasion is inhibited by paclitaxel.

Westerlund, A / Hujanen, E / Höyhtyä, M / Puistola, U / Turpeenniemi-Hujanen, T

Clinical & experimental metastasis

1997 Volume 15, Issue 3, Page(s) 318–328

Abstract: Overproduction of matrix metalloproteinases (MMPs) and alterations in adhesive and migratory behavior are common characteristics of metastatic cancer cells. Ovarian cancer is a highly invasive type of malignancy. The effect of the antineoplastic drug ... ...

Abstract	Overproduction of matrix metalloproteinases (MMPs) and alterations in adhesive and migratory behavior are common characteristics of metastatic cancer cells. Ovarian cancer is a highly invasive type of malignancy. The effect of the antineoplastic drug paclitaxel on human ovarian cancer cell (Ovcar-3) invasion was studied using an in vitro invasion assay with reconstituted basement membrane. The effect of treatment with paclitaxel was also determined separately on certain invasion-associated events, such as the secretion of 72 kDa type IV collagenase (gelatinase A/MMP-2), the expression of the tissue inhibitor of metalloproteinase-2 (TIMP-2), cell attachment and migration. Ovcar-3 cell attachment, migration and in vitro invasion were significantly decreased after paclitaxel treatment (P = 0.02, P < 0.01 and P = 0.001, respectively) whereas no alteration in the secretion of latent MMP-2 was noted. However, the intracellular localization of the immunoreactive protein for MMP-2 was altered in response to paclitaxel treatment. Interestingly, paclitaxel increased the appearance of TIMP-2 protein in culture medium (P = 0.002) but did not change the expression of mRNA for TIMP-2 in Ovcar-3 cells. These data show that paclitaxel is an effective suppressor of Ovcar-3 cell invasion. It inhibits attachment and migratory activities of the cells but also causes a release of TIMP-2 protein into the tissue culture medium.
MeSH term(s)	Antineoplastic Agents, Phytogenic/pharmacology ; Cell Movement/drug effects ; Female ; Gelatinases/analysis ; Gelatinases/metabolism ; Humans ; Matrix Metalloproteinase 2 ; Metalloendopeptidases/analysis ; Microtubules/drug effects ; Neoplasm Invasiveness ; Ovarian Neoplasms/pathology ; Paclitaxel/pharmacology ; Proteins/analysis ; Proteins/genetics ; RNA, Messenger/analysis ; Tissue Inhibitor of Metalloproteinase-2 ; Tumor Cells, Cultured
Chemical Substances	Antineoplastic Agents, Phytogenic ; Proteins ; RNA, Messenger ; Tissue Inhibitor of Metalloproteinase-2 (127497-59-0) ; Gelatinases (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-) ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Paclitaxel (P88XT4IS4D)
Language	English
Publishing date	1997-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604952-7
ISSN	0262-0898
ISSN	0262-0898
DOI	10.1023/a:1018481617275
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Article: Laminin-5 promotes adhesion and migration of epithelial cells: identification of a migration-related element in the gamma2 chain gene (LAMC2) with activity in transgenic mice.

Salo, S / Haakana, H / Kontusaari, S / Hujanen, E / Kallunki, T / Tryggvason, K

Matrix biology : journal of the International Society for Matrix Biology

1997 Volume 18, Issue 2, Page(s) 197–210

Abstract: The effects of laminin-5 and its subunit gamma2 chain on cell adhesion and migration were studied, and a migration-related cis-acting element was identified in the gamma2 chain gene (LAMC2) using promoter-reporter gene constructs in transgenic mice. ... ...

Abstract	The effects of laminin-5 and its subunit gamma2 chain on cell adhesion and migration were studied, and a migration-related cis-acting element was identified in the gamma2 chain gene (LAMC2) using promoter-reporter gene constructs in transgenic mice. Intact laminin-5 molecules, but not recombinant gamma2 chain promoted cell adhesion of human keratinocytes and mouse squamous carcinoma cells, indicating that the gamma2 chain does not contain a cellular binding site. However, the gamma2 chain as such is probably involved in the process of cell locomotion, as antibodies against the short arm of the chain inhibited migration of carcinoma cells in an in vitro assay. Further evidence for the involvement of the gamma2 chain in cell migration was obtained by the identification of a cis-acting element in a promoter-lacZ reporter gene construct that was active in migratory epithelial cells of healing wounds in mice made transgenic by microinjection of the construct into fertilized oozytes. The migration active element was located in the sequence between -613 and +55. The same construct, and another one containing 5900 base pairs of the 5' flanking region, yielded very limited expression in cells of normal tissues. The limited expression was, however, only observed in epithelial cells of different tissues, i.e. cell types that normally express laminin-5 in vivo. The results show that the sequence between -613 and +55 contains elements that can drive expression during epithelial cell migration and that also partially confers more general epithelium expression. However, elements outside -5900 and +55 are needed for normal epithelium expression of the LAMC2 gene.
MeSH term(s)	Animals ; Base Sequence ; Binding Sites ; Cell Adhesion ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/physiology ; Cell Line ; Cell Movement ; DNA, Complementary ; Epithelial Cells/physiology ; Gene Expression ; Genes, Reporter ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mice, Transgenic ; Molecular Sequence Data ; Promoter Regions, Genetic ; Rabbits ; Recombinant Fusion Proteins/metabolism ; Tumor Cells, Cultured ; Kalinin
Chemical Substances	Cell Adhesion Molecules ; DNA, Complementary ; Recombinant Fusion Proteins
Language	English
Publishing date	1997-04-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/s0945-053x(99)00012-8
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Article: Variance in the enzymatic properties of the chloride-activated arginine aminopeptidase from erythrocytes of healthy humans.

Söderling, E / Hujanen, E / Mäkinen, K K

Biochemical medicine

1981 Volume 26, Issue 2, Page(s) 231–238

MeSH term(s)	Aminopeptidases/antagonists & inhibitors ; Aminopeptidases/blood ; Aminopeptidases/immunology ; Chlorides/pharmacology ; Chloromercuribenzoates/pharmacology ; Enzyme Activation/drug effects ; Erythrocytes/enzymology ; Female ; Humans ; Kinetics ; Male ; Substrate Specificity ; p-Chloromercuribenzoic Acid
Chemical Substances	Chlorides ; Chloromercuribenzoates ; p-Chloromercuribenzoic Acid (59-85-8) ; Aminopeptidases (EC 3.4.11.-) ; aminopeptidase B (EC 3.4.11.6)
Language	English
Publishing date	1981-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	391807-5
ISSN	0006-2944
ISSN	0006-2944
DOI	10.1016/0006-2944(81)90050-8
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Zs.A 617: Show issues

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Article: Polymorphonuclear leukocyte chemotaxis induced by zinc, copper and nickel in vitro.

Hujanen, E S / Seppä, S T / Virtanen, K

Biochimica et biophysica acta

1995 Volume 1245, Issue 2, Page(s) 145–152

Abstract: Metallic dental restorations and prosthetic constructions are susceptible to corrosion in oral environment, resulting in the release of various heavy metal ions. Chloride salts of zinc, copper, nickel, chromium, iron and gold were tested for their ... ...

Abstract	Metallic dental restorations and prosthetic constructions are susceptible to corrosion in oral environment, resulting in the release of various heavy metal ions. Chloride salts of zinc, copper, nickel, chromium, iron and gold were tested for their ability to promote the migration of polymorphonuclear leukocytes (PMNs). Using a modified Boyden chamber assay for chemotaxis zinc, copper and nickel enhanced the migration of PMN cells in concentration range of 0.5-1.0 mM, whereas no augmentation in migratory activity was noted using chromium or iron. In contrast, an inhibition in migratory activity was observed in cells directed toward gold ions. Exposure of cells to zinc, copper or nickel ions induced an orientation reaction in leukocytes in a similar fashion as the polarization reaction induced by a potent peptide chemoattractant, N-formylmethionylleucylphenylalanine (fMLP), in these cells. Exposure of PMN cells to zinc or nickel in chemotactic concentrations stimulated the chemotaxis of these cells to fMLP 2-fold, whereas pretreatment of the cells with zinc prior to assay markedly decreased the subsequent chemotactic migration of the cells to this metal or to fMLP. The enhanced locomotion of PMN cells induced by zinc, copper or nickel ions was found to be in greater extent due to an increase in directed migration (chemotaxis) rather than an augmentation in random movement (chemokinesis) as assessed by Zigmond-Hirsch checkerboard analysis. These results suggest that zinc, copper and nickel ions attract leukocytes by inducing and promoting the chemotactic response in these cells, which may modulate the inflammatory response of host tissue around such metals.
MeSH term(s)	Animals ; Cell Adhesion/drug effects ; Cell Polarity/drug effects ; Chemotaxis, Leukocyte/drug effects ; Chromium/pharmacology ; Copper/pharmacology ; Female ; Iron/pharmacology ; Microscopy, Electron, Scanning ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/physiology ; Nickel/pharmacology ; Rats ; Zinc/pharmacology
Chemical Substances	Chromium (0R0008Q3JB) ; N-Formylmethionine Leucyl-Phenylalanine (59880-97-6) ; Copper (789U1901C5) ; Nickel (7OV03QG267) ; Iron (E1UOL152H7) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	1995-10-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/0304-4165(95)00082-m
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Article: Migration of tumor cells to organ-derived chemoattractants.

Hujanen, E S / Terranova, V P

Cancer research

1985 Volume 45, Issue 8, Page(s) 3517–3521

Abstract: Certain tissues contain unique factors which are chemotactic for metastatic tumor cell lines. Extracts of bone, brain, liver, and lung were tested for their ability to promote either the migration or the chemoinvasion, i.e., their penetration through a ... ...

Abstract	Certain tissues contain unique factors which are chemotactic for metastatic tumor cell lines. Extracts of bone, brain, liver, and lung were tested for their ability to promote either the migration or the chemoinvasion, i.e., their penetration through a reconstituted basement membrane barrier, of various metastatic tumor cells. Using a modified Boyden chamber assay for chemotaxis, B16-Br2 melanoma cells, which metastasize to brain, migrated most actively to brain extract. Lung-directed T241-PM2 fibrosarcoma cells migrated selectively to lung extract. Further, murine M50-76 reticulum cell sarcoma cells, which metastasize to liver and ovaries, were preferentially attracted to liver extract, and MCF-7 breast adenocarcinoma cells with high bone and brain colonization potential were found to migrate most actively to bone and brain extracts. Partial purification of tissue extracts showed that the factors in brain and liver are of different molecular weights. These data suggest that tissue-specific factors in different target tissues attract tumor cells which home to those sites.
MeSH term(s)	Animals ; Brain Chemistry ; Cell Line ; Chemotactic Factors/analysis ; Chemotactic Factors/physiology ; Chromatography, Agarose ; Female ; Liver/analysis ; Mice ; Mice, Inbred C57BL ; Molecular Weight ; Neoplasm Invasiveness ; Neoplasm Metastasis/pathology
Chemical Substances	Chemotactic Factors
Language	English
Publishing date	1985-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
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Article: Modulation of type-IV collagenase activity and invasive behavior of metastatic human melanoma (A2058) cells in vitro by monoclonal antibodies to type-IV collagenase.

Höyhtyä, M / Hujanen, E / Turpeenniemi-Hujanen, T / Thorgeirsson, U / Liotta, L A / Tryggvason, K

International journal of cancer

1990 Volume 46, Issue 2, Page(s) 282–286

Abstract: Monoclonal antibodies (MAbs) against human type-IV collagenase were developed and used for studies on enzyme activity and tumor-cell invasion in vitro. Fifteen MAb clones were generated against the enzyme purified form serum-free culture medium of human ... ...

Abstract	Monoclonal antibodies (MAbs) against human type-IV collagenase were developed and used for studies on enzyme activity and tumor-cell invasion in vitro. Fifteen MAb clones were generated against the enzyme purified form serum-free culture medium of human melanoma cells (A2058). Five clones affecting the activity of type-IV collagenase were selected for further characterization. All the selected clones could be used for a single-step purification of type-IV collagenase using IgG-Sepharose affinity columns. One of the antibodies activated the enzyme when 3H-proline-labelled type-IV collagen was used as substrate. The activation was dependent on the enzyme antibody ratio. Four clones caused more than 30% inhibition of the activity, maximal inhibition being 50%. Interestingly, the same antibody which activated the enzyme also increased the invasion of A2058 cells through a reconstituted basement membrane in an in vitro invasion assay. The 4 inhibitory antibodies decreased the penetration of A2058 cells through the reconstituted basement membrane. The results strongly support previous findings about the importance of type-IV collagenase in tumor-cell invasion.
MeSH term(s)	Antibodies, Monoclonal/isolation & purification ; Antibodies, Monoclonal/pharmacology ; Antibody Specificity ; Cell Line ; Clone Cells/enzymology ; Clone Cells/pathology ; Collagen/metabolism ; Enzyme-Linked Immunosorbent Assay ; Humans ; Infant, Newborn ; Melanoma/enzymology ; Melanoma/pathology ; Microbial Collagenase/immunology ; Microbial Collagenase/metabolism ; Neoplasm Invasiveness ; Substrate Specificity ; Tumor Cells, Cultured/enzymology ; Tumor Cells, Cultured/pathology
Chemical Substances	Antibodies, Monoclonal ; Collagen (9007-34-5) ; Microbial Collagenase (EC 3.4.24.3)
Language	English
Publishing date	1990-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218257-9
ISSN	1097-0215 ; 0020-7136
ISSN (online)	1097-0215
ISSN	0020-7136
DOI	10.1002/ijc.2910460224
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