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Action of Proteolytic Enzymes on Tropocollagen and Insoluble Collagen*
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAction of Proteolytic Enzymes on Tropocollagen and Insoluble Collagen*M. P. Drake, P. F. Davison, S. Bump, and F. O. SchmittCite this: Biochemistry 1966, 5, 1, 301–312Publication Date (Print):January 1, 1966Publication History Published online1 May 2002Published inissue 1 January 1966https://pubs.acs.org/doi/10.1021/bi00865a039https://doi.org/10.1021/bi00865a039research-articleACS PublicationsRequest reuse permissionsArticle Views477Altmetric-Citations192LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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“This indicates that dECM from 0.3% concentration has undergone partial cleavage at the telopeptide where most of the intra- and intermolecular crosslinks are found in collagen [59].”
From Effects of Various Decellularization Methods for the Development of Decellularized Extracellular Matrix from Tilapia (Oreochromis niloticus) Viscera (2024) · cites this paper as [59]
Citations
Cites
The Native and Denatured States of Soluble Collagen
Boedtker, H., & Doty, P. M. (1956) · Journal of the American Chemical Society · doi:10.1021/ja01598a024 · Cited by 332
Effects of Pepsin Treatment on the Interaction Properties of Tropocollagen Macromolecules*
Rubin, A. L., Drake, M. P., Davison, P. F., Pfahl, D., Speakman, P. T., & Schmitt, F. O. (1965) · Biochemistry · doi:10.1021/bi00878a001 · Cited by 186
Self-citationTropocollagen: Significance of Protease-Induced Alterations
Rubin, A. L., Pfahl, D., Speakman, P. T., Davidson, P. F., & Schmitt, F. O. (1963) · Science · doi:10.1126/science.139.3549.37 · Cited by 170
Self-citationHall, C. E., & Doty, P. M. (1958) · Journal of the American Chemical Society · doi:10.1021/ja01539a001 · Cited by 152
Subunits of the collagen molecule
Piez, K. A., Lewis, M. S., Martin, G. R., & Gross, J. (1961) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0006-3002(61)90226-8 · Cited by 136
Veis, A., & Drake, M. P. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67933-5 · Cited by 85
Self-citationThe Physical Characterization of Monomeric Tropocollagen*
Davison, P. F., & Drake, M. P. (1966) · Biochemistry · doi:10.1021/bi00865a040 · Cited by 70
Self-citationThe Unusual Links and Cross-Links of Collagen
Harding, J. J. (1965) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60389-7 · Cited by 67
The Precipitation of Collagen Fibers from Solution
Wood, G. C. (1964) · International review of connective tissue research · doi:10.1016/b978-1-4831-6751-0.50007-0 · Cited by 66
Concerning Some Special Structural Features of the Collagen Molecule
Gallop, P. M. (1964) · Biophysical Journal · doi:10.1016/s0006-3495(64)86929-0 · Cited by 57
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Jelínková, M., Stuchlíková, E., & Málková, H. (1969) · Experimental Gerontology · doi:10.1016/0531-5565(69)90024-2 · Cited by 6
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Deyl, Z., Rosmus, J., & Adam, M. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80062-5 · Cited by 5
Solubilization of intact collagen from hamster and baboon lung
Stock, J. W., Henning, M. C., & Collins, J. F. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90198-6 · Cited by 5
Interaction of platelets with collagen modified by irradiation or partial proteolysis
Jeleńska, M., Wegrzynowicz, Z., Dancewicz, A. M., & Kopeć, M. (1973) · Thrombosis Research · doi:10.1016/0049-3848(73)90079-0 · Cited by 5
Some Properties of Insoluble Bovine Corneal Collagen
Šulcová, H., Praus, R., Deyl, Z., Goldman, J. N., & Rosmus, J. (1972) · Connective Tissue Research · doi:10.3109/03008207209152051 · Cited by 5
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Ersinger, V. F. A., Lamas, D. L., & Massa, Á. E. (2025) · Environmental Science and Pollution Research · doi:10.1007/s11356-025-36684-x · Cited by 5
The Seventh Frederick H. Verhoeff Lecture. Collagenase and collagenase inhibitors.
François, J. (1977) · Europe PMC (PubMed Central) · Cited by 4
COLLAGEN CHEMISTRY IN RELATION TO ISINGLASS AND ISINGLASS FININGS. PART II
Leach, A. A., & Barrett, J. (1967) · Journal of the Institute of Brewing · doi:10.1002/j.2050-0416.1967.tb03057.x · Cited by 4
Nonspecific collagenolytic activity: Hydrolysis of native collagen by a mold protease
Nordwig, A., & BRETSCHNEIDER, G. (1971) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(71)90197-5 · Cited by 4
Intermolecular Relationship between Neutral-salt-soluble and Acid-soluble Collagen
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On the presence and localization of an unknown ninhydrin positive compound in ageing collagen
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Fractionation of pepsin-digested, denatured collagen
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McKenzie, J. C., Belton, J. C., & Klein, R. M. (1981) · Journal of Supramolecular Structure and Cellular Biochemistry · doi:10.1002/jsscb.1981.380150303 · Cited by 4
Further studies on the chromatographic separation of the collagen molecular subunits
Cooper, D. R., & Davidson, R. J. (1968) · Journal of Chromatography A · doi:10.1016/0021-9673(68)80064-0 · Cited by 4
Studies on the structure of collagen III1. On the presence of α-keto acids in collagen
Rosmus, J., & Deyl, Z. (1967) · Cellular and Molecular Life Sciences · doi:10.1007/bf02144149 · Cited by 4
Woodlock, A. F., & Harrap, B. S. (1969) · International Journal of Protein Research · doi:10.1111/j.1399-3011.1969.tb01630.x · Cited by 3
Chemical Modification of Collagen and the Effects on Enzyme-Binding: Mechanistic Considerations
Giacin, J. R., & Gilbert, S. G. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-3282-4_28 · Cited by 3
On the interaction between basic telopeptides and DNA
Deyl, Z., Málková, H., & Rosmus, J. (1967) · Cellular and Molecular Life Sciences · doi:10.1007/bf02154136 · Cited by 3
Optical characterization of orientation of collagen
Chang, E. P., & Chien, J. C. W. (1973) · Biopolymers · doi:10.1002/bip.1973.360121209 · Cited by 3
Immunological properties of glomerular basement membrane antigens solubilized by elastase digestion
Stuffers-Heiman, M., Tjoeng-Mutsaerts, N., Ferwerda, W., & van Es, L. A. (1980) · Journal of Immunological Methods · doi:10.1016/0022-1759(80)90120-9 · Cited by 3
The role of the telopeptide region of collagen in the platelet-collagen interaction
Chesney, C. M., Pifer, D. D., Dabbous, M. K., & Brinkley, B. (1979) · Thrombosis Research · doi:10.1016/0049-3848(79)90253-6 · Cited by 3
2.24 Hydrogels of Decellularized Matrix
White, L. J., Saldin, L. T., Keane, T. J., Cramer, M. C., Shakesheff, K. M., & Badylak, S. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803581-8.09313-9 · Cited by 2
Ageing simulating changes in the telopeptide region of the collagen molecule
Rosmus, J., Vančíková, O., & Deyl, Z. (1967) · Experimental Gerontology · doi:10.1016/0531-5565(67)90019-8 · Cited by 2
A Review of the Literature: Collagen: Its Physical Characteristics and Degradation
Weissman, A. M. (1969) · Journal of Periodontology-Periodontics · doi:10.1902/jop.1969.40.10.611 · Cited by 2
Binding of betamethasone and dexamethasone by collagen
Kanfer, I. (1977) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.1977.tb11323.x · Cited by 2
Increased lability of lung collagen crosslinks
Richmond, V. L. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90075-5 · Cited by 2
PLATELET-COLLAGEN INTERACTION AND MICROVESICULATION
Siljander, P. R. M. (2000) · Työväentutkimus Vuosikirja · Cited by 2
Aging of connective tissue. Age dependency of collagen depolymerization by ionizing radiation
Svojtková, E., Deyl, Z., & Adam, M. (1973) · Experimental Gerontology · doi:10.1016/0531-5565(73)90006-5 · Cited by 1
Mineralization of nanomaterials for bone tissue engineering
Marelli, B., Ghezzi, C. E., & Nazhat, S. N. (2013) · Elsevier eBooks · doi:10.1533/9780857097231.3.387 · Cited by 1
Contamination of Acid‐Soluble Collagen with Nitrogenous Material from the Dialysis Tubing
Crevasse, G. A., & PEARSON, A. M. (1969) · Journal of Food Science · doi:10.1111/j.1365-2621.1969.tb14360.x · Cited by 1
Studies on the structure of collagen IV. A.C-terminal sequence from the pronase treated collagen
Bump, S., Deyl, Z., & Rosmus, J. (1967) · Cellular and Molecular Life Sciences · doi:10.1007/bf02137940 · Cited by 1
Self-citationMOCZAR, M., Bessou, J.-P., & Loisance, D. Y. (1983) · Connective Tissue Research · doi:10.3109/03008208309005609 · Cited by 1
Nalinanon, S. (2010) · PSU Knowledge Bank (Prince of Songkla University) · Cited by 1
Design of Collagen-mimetic peptides
Kaur, P. (2017) · CUNY Academic Works (City University of New York) · Cited by 1
Bernengo, J. C., Roux, B., & Herbage, D. (1979) · Springer eBooks · doi:10.1007/978-1-4684-3497-2_24 · Cited by 1
Waheed, H. (2017) · eScholarship@McGill (McGill) · doi:10.82308/7978 · Cited by 1
Corneal Collagenases and their Inhibition
François, J., & Cambie, E. (1976) · Documenta ophthalmologica. Proceedings series · doi:10.1007/978-94-010-1569-1_3
Novel Biofabrication Technologies to Recapitulate In Vivo Geometries in Collagen Hydrogels
Rodriguez-Rivera, V. (2014) · Scholar Commons (University of South Carolina)
The collagenolytic action of the proteolytic complex of streptomyces griseus on synthetic substrates
Rassulin, Y. A., & Шибнев, В. А. (1970) · Russian Chemical Bulletin · doi:10.1007/bf00861504
The absence of α-keto acids in polymeric collagen
Ayad, S., STEVEN, F. S., & Jackson, D. S. (1969) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(69)90079-8
Sama, B. A. (2011) · Digital Repository Service (Northeastern University) · doi:10.17760/d20000956
Diffuse Obstructive Pulmonary Syndromes ENZYME DIGESTION
Martin, C. J., & Sugihara, T. T. (1973)
Segment-long-spacing aggregate from pepsin-solubilized bone collagen.
Kuboki, Y., Sasaki, S., SAITO, J., Ono, T., & Kawanishi, Y. (1973) · PubMed
Spontane Uterusperforation bei Endomyometritis puerperalis durch erh�hten Kollagenabbau
Hertel, H., & Schmitt, W. (1968) · Archives of Gynecology and Obstetrics · doi:10.1007/bf00668074
On the localization of tryptophane in the α3 chain of collagen
Deyl, Z., Rosmus, J., & Málková, H. (1967) · Cellular and Molecular Life Sciences · doi:10.1007/bf02136397
Studies on the inhibition of experimental liver fibrosis
Tsujii, T., Fukuhara, M., Fukuda, S., Matsui, T., Matsuoka, Y., Tamura, M., Morita, T., Kimura, K., & MORIYA, W. (1975) · Gastroenterologia Japonica · doi:10.1007/bf02776655
Inorganic–Organic Hybrids: Mimicking Native Bone
Park, H., Rezabeigi, E., & Nazhat, S. N. (2021) · Royal Society of Chemistry eBooks · doi:10.1039/9781788019828-00134
Collagen-Derived Membrane: Corneal Implantation
Dunn, M. W., Nishihara, T., Stenzel, K. H., Branwood, A. W., & Rubin, A. L. (1967) · Springer eBooks · doi:10.1007/978-1-4615-6555-0_15
Faralizadeh, S., Rahimabadi, E. Z., Bahrami, S. H., & hasannia, S. (2025) · Waste and Biomass Valorization · doi:10.1007/s12649-025-03438-2
Metadata
- Authors
- Drake, M. P., Davison, P. F., Bump, S., & Schmitt, F. O.
- ORCID
- Schmitt, F. O.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1966-01-01
- Volume
- 5
- Issue
- 1
- Pages
- 301-312
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2086460205
- Cited by
- 257
- References
- 20
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 1 · 2014: 3 · 2013: 2 · 2012: 1
- FWCI
- 34.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- proteolytic enzymes, tropocollagen, insoluble collagen, collagen degradation, collagenase
- MeSH terms
- Amino Acids, Animals, Cattle, Chemistry, Chymotrypsin, Collagen, Microscopy, Electron, Pancreatic Elastase, Pepsin A, Peptide Hydrolases, Peptides, Trypsin, Ultracentrifugation, Chemical Phenomena, In Vitro Techniques
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