Monomer and oligomer of type I collagen: molecular properties and fibril assembly
Type I collagen purified from calf skin was further separated into monomeric and oligomeric fractions and characterized with gel electrophoresis and measurement of solution viscosity. The thermal stabilities of the triple-helical structure of the collagen molecules of these preparations and the fibr...
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| Veröffentlicht in: | Biochemistry (Easton) 1989-09, Vol.28 (18), p.7161-7167 |
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| creator | Na, George C |
| description | Type I collagen purified from calf skin was further separated into monomeric and oligomeric fractions and characterized with gel electrophoresis and measurement of solution viscosity. The thermal stabilities of the triple-helical structure of the collagen molecules of these preparations and the fibrils assembled therefrom were determined with differential UV spectroscopy and scanning microcalorimetry. The monomeric collagen was reduced with NaBH4-, and the kinetics and equilibrium of the reversible fibril assembly-disassembly were examined in detail. Fibril assembly and disassembly of the collagen induced by slow scans of temperature showed hysteresis. The assembly curve was very sharp whereas the disassembly curve was gradual. Equilibrium centrifugation showed the collagen disassembled from the fibrils to be predominantly monomers. However, unlike the unassembled collagen, the collagen disassembled from fibrils by cooling showed no lag phase in subsequent cycles of fibril assembly. The thermodynamic parameters of fibril growth were derived from a fibril disassembly curve. Fibril growth was weaker for the NaBH4-reduced monomeric collagen than the native crude collagen, perhaps due to the removal of oligomers and the changes in the molecular structure brought by the reduction. The results corroborated the strongly cooperative mechanism for the fibril assembly proposed in the preceding paper. |
| doi_str_mv | 10.1021/bi00444a005 |
| format | Article |
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The thermal stabilities of the triple-helical structure of the collagen molecules of these preparations and the fibrils assembled therefrom were determined with differential UV spectroscopy and scanning microcalorimetry. The monomeric collagen was reduced with NaBH4-, and the kinetics and equilibrium of the reversible fibril assembly-disassembly were examined in detail. Fibril assembly and disassembly of the collagen induced by slow scans of temperature showed hysteresis. The assembly curve was very sharp whereas the disassembly curve was gradual. Equilibrium centrifugation showed the collagen disassembled from the fibrils to be predominantly monomers. However, unlike the unassembled collagen, the collagen disassembled from fibrils by cooling showed no lag phase in subsequent cycles of fibril assembly. The thermodynamic parameters of fibril growth were derived from a fibril disassembly curve. Fibril growth was weaker for the NaBH4-reduced monomeric collagen than the native crude collagen, perhaps due to the removal of oligomers and the changes in the molecular structure brought by the reduction. The results corroborated the strongly cooperative mechanism for the fibril assembly proposed in the preceding paper.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00444a005</identifier><identifier>PMID: 2819058</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; BIOCHEMISTRY ; BIOCHIMIE ; Biological and medical sciences ; BIOQUIMICA ; Calorimetry, Differential Scanning ; CALVES ; Cattle ; Centrifugation ; COLAGENOS ; COLLAGEN ; Collagen - metabolism ; Collagen - ultrastructure ; COLLAGENE ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Interactions. Associations ; Intermolecular phenomena ; Kinetics ; Macromolecular Substances ; Molecular biophysics ; Oxidation-Reduction ; PROPIEDADES TERMICAS ; PROPRIETE THERMIQUE ; Protein Denaturation ; protein structure ; PROTEINAS ; PROTEINE ; PROTEINS ; skin ; subunits ; Temperature ; TERNERO ; THERMAL PROPERTIES ; Thermodynamics ; VEAU ; VISCOSIDAD ; VISCOSITE ; VISCOSITY</subject><ispartof>Biochemistry (Easton), 1989-09, Vol.28 (18), p.7161-7167</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a500t-c604fc103d51d17877aefe1ef6595332b6006d280589c71a44a96db4ab6485c03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00444a005$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00444a005$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19288343$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2819058$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Na, George C</creatorcontrib><title>Monomer and oligomer of type I collagen: molecular properties and fibril assembly</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Type I collagen purified from calf skin was further separated into monomeric and oligomeric fractions and characterized with gel electrophoresis and measurement of solution viscosity. The thermal stabilities of the triple-helical structure of the collagen molecules of these preparations and the fibrils assembled therefrom were determined with differential UV spectroscopy and scanning microcalorimetry. The monomeric collagen was reduced with NaBH4-, and the kinetics and equilibrium of the reversible fibril assembly-disassembly were examined in detail. Fibril assembly and disassembly of the collagen induced by slow scans of temperature showed hysteresis. The assembly curve was very sharp whereas the disassembly curve was gradual. Equilibrium centrifugation showed the collagen disassembled from the fibrils to be predominantly monomers. However, unlike the unassembled collagen, the collagen disassembled from fibrils by cooling showed no lag phase in subsequent cycles of fibril assembly. The thermodynamic parameters of fibril growth were derived from a fibril disassembly curve. Fibril growth was weaker for the NaBH4-reduced monomeric collagen than the native crude collagen, perhaps due to the removal of oligomers and the changes in the molecular structure brought by the reduction. The results corroborated the strongly cooperative mechanism for the fibril assembly proposed in the preceding paper.</description><subject>Animals</subject><subject>BIOCHEMISTRY</subject><subject>BIOCHIMIE</subject><subject>Biological and medical sciences</subject><subject>BIOQUIMICA</subject><subject>Calorimetry, Differential Scanning</subject><subject>CALVES</subject><subject>Cattle</subject><subject>Centrifugation</subject><subject>COLAGENOS</subject><subject>COLLAGEN</subject><subject>Collagen - metabolism</subject><subject>Collagen - ultrastructure</subject><subject>COLLAGENE</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Molecular biophysics</subject><subject>Oxidation-Reduction</subject><subject>PROPIEDADES TERMICAS</subject><subject>PROPRIETE THERMIQUE</subject><subject>Protein Denaturation</subject><subject>protein structure</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>skin</subject><subject>subunits</subject><subject>Temperature</subject><subject>TERNERO</subject><subject>THERMAL PROPERTIES</subject><subject>Thermodynamics</subject><subject>VEAU</subject><subject>VISCOSIDAD</subject><subject>VISCOSITE</subject><subject>VISCOSITY</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEYhoModVs9eROEuagHGf0y-TXxJou2hRWVtueQySRLamayJjPg_vfNdpbqQfAUwvvkzZMvCL3A8B5Dgz90HoBSqgHYI7TCrIGaSskeoxUA8LqRHJ6i05xvy5aCoCfopGmxBNau0I-vcYyDTZUe-yoGv73fRFdN-52tLisTQ9BbO36shhismYNO1S7FnU2Tt_n-lPNd8qHSOduhC_tn6InTIdvnx_UM3Xz5fL2-qDffzi_Xnza1ZgBTbThQZzCQnuEei1YIbZ3F1nEmGSFNx4t737TFUhqBdXmf5H1HdcdpywyQM_Rm6S06v2abJzX4bGzRHW2csxKytJSr_gtiRinh9AC-W0CTYs7JOrVLftBprzCow6TVX5Mu9Ktj7dwNtn9gj6Mt-etjrrPRwSU9Gp__VMqmbQklhasXzufJ_n7IdfqpuCCCqevvVwqv2YVYnxO1KfzLhXc6Kr1NpfPmSkLxaw5Sb5dQm6xu45zG8gX_1L8DGlGnlg</recordid><startdate>19890905</startdate><enddate>19890905</enddate><creator>Na, George C</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890905</creationdate><title>Monomer and oligomer of type I collagen: molecular properties and fibril assembly</title><author>Na, George C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a500t-c604fc103d51d17877aefe1ef6595332b6006d280589c71a44a96db4ab6485c03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>BIOCHEMISTRY</topic><topic>BIOCHIMIE</topic><topic>Biological and medical sciences</topic><topic>BIOQUIMICA</topic><topic>Calorimetry, Differential Scanning</topic><topic>CALVES</topic><topic>Cattle</topic><topic>Centrifugation</topic><topic>COLAGENOS</topic><topic>COLLAGEN</topic><topic>Collagen - metabolism</topic><topic>Collagen - ultrastructure</topic><topic>COLLAGENE</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Molecular biophysics</topic><topic>Oxidation-Reduction</topic><topic>PROPIEDADES TERMICAS</topic><topic>PROPRIETE THERMIQUE</topic><topic>Protein Denaturation</topic><topic>protein structure</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>skin</topic><topic>subunits</topic><topic>Temperature</topic><topic>TERNERO</topic><topic>THERMAL PROPERTIES</topic><topic>Thermodynamics</topic><topic>VEAU</topic><topic>VISCOSIDAD</topic><topic>VISCOSITE</topic><topic>VISCOSITY</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Na, George C</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Na, George C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monomer and oligomer of type I collagen: molecular properties and fibril assembly</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1989-09-05</date><risdate>1989</risdate><volume>28</volume><issue>18</issue><spage>7161</spage><epage>7167</epage><pages>7161-7167</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Type I collagen purified from calf skin was further separated into monomeric and oligomeric fractions and characterized with gel electrophoresis and measurement of solution viscosity. The thermal stabilities of the triple-helical structure of the collagen molecules of these preparations and the fibrils assembled therefrom were determined with differential UV spectroscopy and scanning microcalorimetry. The monomeric collagen was reduced with NaBH4-, and the kinetics and equilibrium of the reversible fibril assembly-disassembly were examined in detail. Fibril assembly and disassembly of the collagen induced by slow scans of temperature showed hysteresis. The assembly curve was very sharp whereas the disassembly curve was gradual. Equilibrium centrifugation showed the collagen disassembled from the fibrils to be predominantly monomers. However, unlike the unassembled collagen, the collagen disassembled from fibrils by cooling showed no lag phase in subsequent cycles of fibril assembly. The thermodynamic parameters of fibril growth were derived from a fibril disassembly curve. Fibril growth was weaker for the NaBH4-reduced monomeric collagen than the native crude collagen, perhaps due to the removal of oligomers and the changes in the molecular structure brought by the reduction. The results corroborated the strongly cooperative mechanism for the fibril assembly proposed in the preceding paper.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2819058</pmid><doi>10.1021/bi00444a005</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals BIOCHEMISTRY BIOCHIMIE Biological and medical sciences BIOQUIMICA Calorimetry, Differential Scanning CALVES Cattle Centrifugation COLAGENOS COLLAGEN Collagen - metabolism Collagen - ultrastructure COLLAGENE Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Interactions. Associations Intermolecular phenomena Kinetics Macromolecular Substances Molecular biophysics Oxidation-Reduction PROPIEDADES TERMICAS PROPRIETE THERMIQUE Protein Denaturation protein structure PROTEINAS PROTEINE PROTEINS skin subunits Temperature TERNERO THERMAL PROPERTIES Thermodynamics VEAU VISCOSIDAD VISCOSITE VISCOSITY |
| title | Monomer and oligomer of type I collagen: molecular properties and fibril assembly |
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