A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks
Tryptic peptides of bone collagens from 4-week-old normal, osteoblastoma and vitamin D-deficient chicks were studied using gel filtration chromatography. Absorbance at 230 nm and fluorescence (excitation at 330 nm, emission at 390 nm) of each fraction were measured. The relative quantities of each p...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1981-01, Vol.102 (1), p.59-65 |
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| creator | Yamauchi, Mitsuo Banes, Albert J. Kuboki, Yoshinori Mechanic, Gerald L. |
| description | Tryptic peptides of bone collagens from 4-week-old normal, osteoblastoma and vitamin D-deficient chicks were studied using gel filtration chromatography. Absorbance at 230 nm and fluorescence (excitation at 330 nm, emission at 390 nm) of
each
fraction
were measured. The relative quantities of each peak from the absorbance and fluorescence patterns were semiquantified by planimetry. Osteoblastoma bone collagen had a prominent, fluorescent, crosslinked peptide that contained pyridinoline. Fluorescence of this pyridinoline-containing peak in AO collagen was much greater than in the vitamin D-deficient and normal bone collagen counterparts. A comparison of fluorescence patterns clearly showed that the distribution of pyridinoline in collagen from normal and diseased bone was totally dissimilar.
The dissimilarities in distribution of pyridinoline in these bone collagens may be attributed to differences in the degree of lysine hydroxylation, to the degree of mineralization, or some other factor. |
| doi_str_mv | 10.1016/0006-291X(81)91488-1 |
| format | Article |
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each
fraction
were measured. The relative quantities of each peak from the absorbance and fluorescence patterns were semiquantified by planimetry. Osteoblastoma bone collagen had a prominent, fluorescent, crosslinked peptide that contained pyridinoline. Fluorescence of this pyridinoline-containing peak in AO collagen was much greater than in the vitamin D-deficient and normal bone collagen counterparts. A comparison of fluorescence patterns clearly showed that the distribution of pyridinoline in collagen from normal and diseased bone was totally dissimilar.
The dissimilarities in distribution of pyridinoline in these bone collagens may be attributed to differences in the degree of lysine hydroxylation, to the degree of mineralization, or some other factor.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(81)91488-1</identifier><identifier>PMID: 7306173</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids - analysis ; Animals ; Bone and Bones - analysis ; Chickens ; Collagen - analysis ; Cross-Linking Reagents ; Neoplasms, Experimental - analysis ; Osteoma, Osteoid - analysis ; Peptide Fragments - analysis ; Pyridinium Compounds - analysis ; Space life sciences ; Vitamin D Deficiency - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1981-01, Vol.102 (1), p.59-65</ispartof><rights>1981</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-28b9b8c5b615335a5e5d31f7e53fa76a5a1643d5b179107433dee61ee50a8adc3</citedby><cites>FETCH-LOGICAL-c411t-28b9b8c5b615335a5e5d31f7e53fa76a5a1643d5b179107433dee61ee50a8adc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(81)91488-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7306173$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamauchi, Mitsuo</creatorcontrib><creatorcontrib>Banes, Albert J.</creatorcontrib><creatorcontrib>Kuboki, Yoshinori</creatorcontrib><creatorcontrib>Mechanic, Gerald L.</creatorcontrib><title>A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Tryptic peptides of bone collagens from 4-week-old normal, osteoblastoma and vitamin D-deficient chicks were studied using gel filtration chromatography. Absorbance at 230 nm and fluorescence (excitation at 330 nm, emission at 390 nm) of
each
fraction
were measured. The relative quantities of each peak from the absorbance and fluorescence patterns were semiquantified by planimetry. Osteoblastoma bone collagen had a prominent, fluorescent, crosslinked peptide that contained pyridinoline. Fluorescence of this pyridinoline-containing peak in AO collagen was much greater than in the vitamin D-deficient and normal bone collagen counterparts. A comparison of fluorescence patterns clearly showed that the distribution of pyridinoline in collagen from normal and diseased bone was totally dissimilar.
The dissimilarities in distribution of pyridinoline in these bone collagens may be attributed to differences in the degree of lysine hydroxylation, to the degree of mineralization, or some other factor.</description><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Bone and Bones - analysis</subject><subject>Chickens</subject><subject>Collagen - analysis</subject><subject>Cross-Linking Reagents</subject><subject>Neoplasms, Experimental - analysis</subject><subject>Osteoma, Osteoid - analysis</subject><subject>Peptide Fragments - analysis</subject><subject>Pyridinium Compounds - analysis</subject><subject>Space life sciences</subject><subject>Vitamin D Deficiency - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQxi0EKkvhDQD5hEDagCeOY-eCVJW_UiUOUImb5diT1jSJt7az0j4LL4u3u_QIJ2s8v2_s-T5CngN7Cwzad4yxtqo7-PlawZsOGqUqeEBWwDpW1cCah2R1jzwmT1L6xRhA03Yn5ERy1oLkK_L7jNowbUw02W-Rpry4HQ0DzddInU85-n7JPsx_71I2_YjUxpDS6OebNd3sond-DqXCNfUz7cNcgDCO5grnRIcYJjqHOJlxTUPKGPrRpBwms6ZmdnTrs5mK7EPlcPDW45ypvfb2Jj0ljwYzJnx2PE_J5aePP86_VBffPn89P7uobAOQq1r1Xa-s6FsQnAsjUDgOg0TBByNbIwy0DXeiB9kBkw3nDrEFRMGMMs7yU_LqMHcTw-2CKevJJ4tlgRnDkrTkkteyaf4LlvdrVdACNgfwzqeIg95EP5m408D0Pjy9T0bvk9EK9F14GorsxXH-0k_o7kXHtEr_5aE_mKDNVfRJX36HTtVMsUaKPfD-AGCxa-sx6rQ31KLzEW3WLvh__-APgYm0lw</recordid><startdate>19810101</startdate><enddate>19810101</enddate><creator>Yamauchi, Mitsuo</creator><creator>Banes, Albert J.</creator><creator>Kuboki, Yoshinori</creator><creator>Mechanic, Gerald L.</creator><general>Elsevier Inc</general><scope>FBQ</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>19810101</creationdate><title>A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks</title><author>Yamauchi, Mitsuo ; Banes, Albert J. ; Kuboki, Yoshinori ; Mechanic, Gerald L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-28b9b8c5b615335a5e5d31f7e53fa76a5a1643d5b179107433dee61ee50a8adc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Bone and Bones - analysis</topic><topic>Chickens</topic><topic>Collagen - analysis</topic><topic>Cross-Linking Reagents</topic><topic>Neoplasms, Experimental - analysis</topic><topic>Osteoma, Osteoid - analysis</topic><topic>Peptide Fragments - analysis</topic><topic>Pyridinium Compounds - analysis</topic><topic>Space life sciences</topic><topic>Vitamin D Deficiency - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamauchi, Mitsuo</creatorcontrib><creatorcontrib>Banes, Albert J.</creatorcontrib><creatorcontrib>Kuboki, Yoshinori</creatorcontrib><creatorcontrib>Mechanic, Gerald L.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamauchi, Mitsuo</au><au>Banes, Albert J.</au><au>Kuboki, Yoshinori</au><au>Mechanic, Gerald L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1981-01-01</date><risdate>1981</risdate><volume>102</volume><issue>1</issue><spage>59</spage><epage>65</epage><pages>59-65</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Tryptic peptides of bone collagens from 4-week-old normal, osteoblastoma and vitamin D-deficient chicks were studied using gel filtration chromatography. Absorbance at 230 nm and fluorescence (excitation at 330 nm, emission at 390 nm) of
each
fraction
were measured. The relative quantities of each peak from the absorbance and fluorescence patterns were semiquantified by planimetry. Osteoblastoma bone collagen had a prominent, fluorescent, crosslinked peptide that contained pyridinoline. Fluorescence of this pyridinoline-containing peak in AO collagen was much greater than in the vitamin D-deficient and normal bone collagen counterparts. A comparison of fluorescence patterns clearly showed that the distribution of pyridinoline in collagen from normal and diseased bone was totally dissimilar.
The dissimilarities in distribution of pyridinoline in these bone collagens may be attributed to differences in the degree of lysine hydroxylation, to the degree of mineralization, or some other factor.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7306173</pmid><doi>10.1016/0006-291X(81)91488-1</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1981-01, Vol.102 (1), p.59-65 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73732744 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acids - analysis Animals Bone and Bones - analysis Chickens Collagen - analysis Cross-Linking Reagents Neoplasms, Experimental - analysis Osteoma, Osteoid - analysis Peptide Fragments - analysis Pyridinium Compounds - analysis Space life sciences Vitamin D Deficiency - metabolism |
| title | A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks |
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