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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]
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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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Grant, M. E., & Jackson, D. S. (1968) · Biochemical Journal · doi:10.1042/bj1080587 · Cited by 39
Katzman, R. L., & Kang, A. H. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81131-4 · Cited by 38
Pearson, C. H., Wohllebe, M., Carmichael, D., & Chovelon, A. (1975) · Connective Tissue Research · doi:10.3109/03008207509152179 · Cited by 36
The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation
Veis, A., BHATNAGAR, R. S., Shuttleworth, C. A., & Mussell, S. (1970) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(70)90048-6 · Cited by 36
Sun, W., Yang, Y., Wang, L., Tang, H., Zhang, L., She, Y., Xiao, X., Hu, X., Feng, Q., & Chen, C. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202201257 · Cited by 35
Influence of the telopeptides on type I collagen fibrillogenesis
Brennan, M., & Davison, P. F. (1981) · Biopolymers · doi:10.1002/bip.1981.360201012 · Cited by 35
Self-citationSolid-State Characterization of the Structure and Property of Collagen
Chien, J. C. W. (1975) · Journal of macromolecular science. Part C, Reviews in macromolecular chemistry and physics/Journal of macromolecular science. Reviews in macromolecular chemistry and physics · doi:10.1080/15321797508076103 · Cited by 35
Cell adhesion to collagenous matrices
McCarthy, J. B., Vachhani, B., & Iida, J. (1996) · Biopolymers · doi:10.1002/(sici)1097-0282(1996)40:4 · Cited by 41
Otter, A., Kotovych, G., & Scott, P. G. (1989) · Biochemistry · doi:10.1021/bi00446a006 · Cited by 34
TRANSFORMATIONS OF RAT SKIN COLLAGEN WITH SPECIAL REFERENCE TO THE AGEING PROCESS
Heikkinen, E. M. (1968) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1968.tb04317.x · Cited by 34
Investigation on the Reaction of Metals with Collagen in vivo
Deyl, Z., Rosmus, J., & Adam, M. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00965.x · Cited by 33
Schwarz, W., & G�ldner, F.-H. (1967) · Cell and Tissue Research · doi:10.1007/bf00336868 · Cited by 33
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Lin, A. H., Zitnay, J. L., Li, Y., Yu, S. M., & Weiss, J. A. (2018) · Journal of Orthopaedic Research® · doi:10.1002/jor.24185 · Cited by 32
Collagen-Derived Membrane: Corneal Implantation
Dunn, M. W., Nishihara, T., Stenzel, K. H., Branwood, A. W., & Rubin, A. L. (1967) · Science · doi:10.1126/science.157.3794.1329 · Cited by 32
β-Aspartylglycine in urine and enzymic hydrolyzates of proteins
Pisano, J. J., Prado, E. S., & Freedman, J. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90427-9 · Cited by 32
Hart, G. J., Russell, A. E., & Cooper, D. R. (1971) · Biochemical Journal · doi:10.1042/bj1250599 · Cited by 31
Description of collagen fibril formation by a theory of polymer crystallization
Wallace, D. G., & Thompson, A. Y. (1983) · Biopolymers · doi:10.1002/bip.360220713 · Cited by 31
Pearson, C. H., Happey, F., Naylor, A., Turner, R. L., Palframan, J., & Shentall, R. D. (1972) · Annals of the Rheumatic Diseases · doi:10.1136/ard.31.1.45 · Cited by 30
The effect of γ-irradiation on soluble collagen
Davidson, R. J., & Cooper, D. R. (1968) · Biochemical Journal · doi:10.1042/bj1070029 · Cited by 30
Molecular pathogenesis of root dentin caries
Dung, T. V., & Liu, A. (1999) · Oral Diseases · doi:10.1111/j.1601-0825.1999.tb00071.x · Cited by 30
Inter- and Intramolecular Cross-linking in Tyrosinase-treated Tropocollagen
Dabbous, M. K. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96431-8 · Cited by 30
The effects of acetic acid and pepsin on the crosslinkages and ultrastructure of corneal collagen
Lian, J. B., Morris, S. M., Faris, B., Albright, J. T., & Franzblau, C. (1973) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(73)90345-0 · Cited by 29
Snowden, J. M., & Swann, D. A. (1979) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(79)90149-1 · Cited by 29
Connective Tissue Damage in Emphysema
JOHANSON, W. G., Reynolds, R. C., Scott, T. C., & Pierce, A. K. (1973) · American Review of Respiratory Disease · doi:10.1164/arrd.1973.107.4.589 · Cited by 29
The Degradation of Human Dentine Collagen by Trypsin
Scott, P. G., & Leaver, A. G. (1974) · Connective Tissue Research · doi:10.3109/03008207409152259 · Cited by 28
Heterogeneity of collagens from basement membranes of lens and cornea
Davison, P. F., & Cannon, D. J. (1977) · Experimental Eye Research · doi:10.1016/0014-4835(77)90125-7 · Cited by 28
Self-citationChemical Synthesis of Peptides Containing Site-Specific Advanced Glycation Endproducts
Kaur, H., Kamalov, M., & Brimble, M. A. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.6b00366 · Cited by 27
Almalla, A., Elomaa, L., Bechtella, L., Daneshgar, A., Yavvari, P. S., Mahfouz, Z., Tang, P., Koksch, B., Sauer, I. M., Pagel, K., et al. (2023) · Biomacromolecules · doi:10.1021/acs.biomac.3c00602 · Cited by 26
Degradation of bovine incisor root collagen in an in vitro caries model
Klont, B., Damen, J. J. M., & ten Cate, J. M. (1991) · Archives of Oral Biology · doi:10.1016/0003-9969(91)90100-9 · Cited by 26
Exclusion of dextrans by meshworks of collagenous fibres
Pearce, R. H., & Laurent, T. C. (1977) · Biochemical Journal · doi:10.1042/bj1630617 · Cited by 26
Kaur, P. J., Strawn, R., Bai, H., Xu, K., Ordas, G., Matsui, H., & Xu, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.542241 · Cited by 25
Zagari, A., Palmer, K. A., Gibson, K. D., Némethy, G., & Scheraga, H. A. (1994) · Biopolymers · doi:10.1002/bip.360340107 · Cited by 25
Collagen: Relatively Invariant (Helical) and Variable (Nonhelical) Regions
BORNSTEIN, P. K. (1968) · Science · doi:10.1126/science.161.3841.592 · Cited by 25
Isolation and chemical characterization of collagen in bovine pulmonary tissues
Francis, G. E., & Thomas, J. P. (1975) · Biochemical Journal · doi:10.1042/bj1450287 · Cited by 24
A fluorescent compound in collagen and its relation to the age of the animal
Deyl, Z., Šulcová, H., Praus, R., & Goldman, J. N. (1970) · Experimental Gerontology · doi:10.1016/0531-5565(70)90029-x · Cited by 24
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Chomarat, N., Robert, L., Séris, J.-L., & Kern, P. (1994) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(94)90032-9 · Cited by 23
Deyl, Z., Praus, R., Šulcová, H., & Goldman, J. N. (1969) · FEBS Letters · doi:10.1016/0014-5793(69)80328-5 · Cited by 22
Veis, A., Brownell, A. G., & Kefalides, N. A. (1975) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409237509102549 · Cited by 22
Collagen from the giant acanthocephalan Macracanthorhynchus hirudinaceus
Cain, G. D. (1970) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(70)90131-1 · Cited by 22
Corneal Collagenase: Specific Cleavage of Types (α1)2α2 and (α1)3Collagens
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Self-citationSingle-stage partial depolymerisation of collagen fibrils
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Bone morphogenesis in implants of residues of radioisotope labelled bone matrix
Urist, M. R., Earnest, F., Kimball, K. M., Julio, T. P., & Iwata, H. (1974) · Calcified Tissue International · doi:10.1007/bf02059062 · Cited by 21
Heterogeneity of tropocollagen as investigated by chromatography on hydroxyapatite columns
川崎, 力., & Bernardi, G. (1970) · Biopolymers · doi:10.1002/bip.1970.360090304 · Cited by 21
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Kamalov, M., Harris, P. W. R., Cooper, G. J. S., & Brimble, M. A. (2014) · Chemical Communications · doi:10.1039/c4cc02003k · Cited by 20
Intermolecular interaction studies on native and enzyme-treated acid-soluble collagen
Bernengo, J. C., Herbage, D., Marion, C., & Roux, B. (1978) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(78)90585-8 · Cited by 19
Nordwig, A. (1971) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122792.ch4 · Cited by 19
Kelly, P. T., von der Mark, K., & Conrad, G. W. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90267-0 · Cited by 19
Studies on the structure of collagen
Rosmus, J., Deyl, Z., & Drake, M. P. (1967) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(67)90524-7 · Cited by 19
Self-citationScanning electron microscope observations on collagen fibers in human dentin and pulp
SÖGAARD‐PEDERSEN, B., Boye, H., & MATTHIESSEN, M. E. (1990) · European Journal Of Oral Sciences · doi:10.1111/j.1600-0722.1990.tb00945.x · Cited by 18
Multiple-stage depolymerisation of collagen fibrils
STEVEN, F. S. (1966) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(66)90025-0 · Cited by 17
A simple vertebrate collagenase assay using soluble radioactive collagen substrate
Seng, W. L., Davison, P. F., & Kenyon, K. R. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90384-1 · Cited by 17
Self-citationHomeostasis in Extracellular Tissues: Insights from Studies on Collage
Davison, P. F., & Harris, E. D. (1973) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409237309102547 · Cited by 17
Self-citationCOLLAGEN CHEMISTRY IN RELATION TO ISINGLASS AND ISINGLASS FININGS-A REVIEW
Leach, A. A. (1967) · Journal of the Institute of Brewing · doi:10.1002/j.2050-0416.1967.tb03011.x · Cited by 16
Preparation and properties of an apoprotein derivative of human serum β‐lipoprotein
Gotto, A. M., Levy, R. I., & Fredrickson, D. S. (1968) · Lipids · doi:10.1007/bf02530887 · Cited by 16
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Ghosh, S. K., & Hp, M. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90099-9 · Cited by 15
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Athenstaedt, H. (1969) · Cell and Tissue Research · doi:10.1007/bf00338332 · Cited by 15
Švadlenka, I., Davídková, E., & Rosmus, J. (1975) · European Food Research and Technology · doi:10.1007/bf01139539 · Cited by 15
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LIN, P. M., Giacin, J. R., Leeder, J., GILBERT, S. G., & WANG, S. (1976) · Journal of Food Science · doi:10.1111/j.1365-2621.1976.tb14388.x · Cited by 11
Chien, J. C. W., & Chang, E. P. (1973) · Biopolymers · doi:10.1002/bip.1973.360120911 · Cited by 11
Carmichael, D., Dodd, C. M., & Veis, A. (1977) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(77)90054-x · Cited by 11
Liu, X., Scott, P. G., Otter, A., & Kotovych, G. (1990) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1990.10507790 · Cited by 11
Martin, C. J., & Sugihara, T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107375 · Cited by 11
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Primary structure of insoluble tendon collagen
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Primary structure of insoluble tendon collagen
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Worrall, J., & STEVEN, F. S. (1966) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(66)90022-5 · Cited by 8
Aldehyde content of collagen from alcoholic cirrhotic and noncirrhotic human livers
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Müller, P., & Kühn, K. (1968) · FEBS Letters · doi:10.1016/0014-5793(68)80070-5 · Cited by 8
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STEVEN, F. S., Grant, M. E., Ayad, S., Weiss, J. B., & Leibovich, S. J. (1970) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(70)90321-1 · Cited by 8
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Deyl, Z. (1968) · Experimental Gerontology · doi:10.1016/0531-5565(68)90017-x · Cited by 8
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Hong, H., Eom, S., Lee, S. J., Youn, J., Kim, D., Chong, H. B., & Kim, D. S. (2022) · International Journal of Precision Engineering and Manufacturing · doi:10.1007/s12541-021-00615-w · Cited by 7
Sanli, A., Elibol, C., & Aydınoğlu, A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823797-7.00004-6 · Cited by 7
Limited Degradation of Gelatin Substrate by Cathepsin D
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Steffen, C., Timpl, R., Wolff, I., & Furthmayr, H. (1970) · PubMed Central · Cited by 7
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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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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