Zobrazeno 1 - 10
of 22
pro vyhledávání: '"R E Boynton"'
Publikováno v:
Journal of Biological Chemistry. 269:21547-21554
A leucine-rich protein, chondroadherin, has been isolated from dissociative extracts of articular cartilage, and its primary structure has been determined by both direct protein sequencing and DNA sequence analysis of polymerase chain reaction produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df19ea4363bc75b870dbe76663c4e6a8
https://doi.org/10.1016/s0021-9258(17)31839-2
https://doi.org/10.1016/s0021-9258(17)31839-2
Publikováno v:
The Yale Journal of Biology and Medicine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::77989d6cad406374e30014d83e60dc37
https://pubmed.ncbi.nlm.nih.gov/21434077
https://pubmed.ncbi.nlm.nih.gov/21434077
Autor:
R E, BOYNTON
Publikováno v:
Occupational medicine. 2(6)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c1f6db35bcf006d9256815c795197a45
https://pubmed.ncbi.nlm.nih.gov/20288143
https://pubmed.ncbi.nlm.nih.gov/20288143
Publikováno v:
Journal of Biological Chemistry. 266:8198-8205
A method has been developed for the production, isolation, and quantitation of 15 marker peptides from the three globular domains (G1, G2, and G3) and the interglobular domain of bovine aggrecan (aggregating cartilage proteoglycan). Three of the pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::792beae5f559d65b91af201b74d6d79a
https://doi.org/10.1016/s0021-9258(18)92961-3
https://doi.org/10.1016/s0021-9258(18)92961-3
Publikováno v:
Journal of Biological Chemistry. 266:8683-8685
The catabolism of aggrecan has been studied in calf articular cartilage explant cultures. The chondroitin sulfate-rich, high buoyant density products that accumulate in culture medium have been purified, and NH2-terminal sequence data have been obtai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::26a35f4f5485952a16ca99b43a275848
https://doi.org/10.1016/s0021-9258(18)31499-6
https://doi.org/10.1016/s0021-9258(18)31499-6
Publikováno v:
The Journal of biological chemistry. 272(22)
Analysis of the carboxymethylated subunit of human cartilage oligomeric matrix protein (COMP) by matrix-assisted laser desorption time-of-flight mass spectrometry indicated a protonated molecular mass of 86949 +/- 149 Da, compared with 83547.0 Da cal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::378c8a91faa0da15a7c1d8fff218e6c3
https://pubmed.ncbi.nlm.nih.gov/9162039
https://pubmed.ncbi.nlm.nih.gov/9162039
Publikováno v:
The Journal of biological chemistry. 269(34)
A leucine-rich protein, chondroadherin, has been isolated from dissociative extracts of articular cartilage, and its primary structure has been determined by both direct protein sequencing and DNA sequence analysis of polymerase chain reaction produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b606b59acba4deaf53c2067e87fb0876
https://pubmed.ncbi.nlm.nih.gov/8063792
https://pubmed.ncbi.nlm.nih.gov/8063792
Publikováno v:
The Journal of biological chemistry. 266(14)
The catabolism of aggrecan has been studied in calf articular cartilage explant cultures. The chondroitin sulfate-rich, high buoyant density products that accumulate in culture medium have been purified, and NH2-terminal sequence data have been obtai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::07496f68e2f3f35b6b17447e33ac612b
https://pubmed.ncbi.nlm.nih.gov/2026585
https://pubmed.ncbi.nlm.nih.gov/2026585
Publikováno v:
The Journal of biological chemistry. 266(13)
A method has been developed for the production, isolation, and quantitation of 15 marker peptides from the three globular domains (G1, G2, and G3) and the interglobular domain of bovine aggrecan (aggregating cartilage proteoglycan). Three of the pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::75cb534a4d424e14b9f30e7c8c615317
https://pubmed.ncbi.nlm.nih.gov/2022637
https://pubmed.ncbi.nlm.nih.gov/2022637
Publikováno v:
The Journal of biological chemistry. 265(34)
The aggregating cartilage proteoglycan core protein contains two globular domains near the N terminus (G1 and G2) and one near the C terminus (G3). The G1-G3 domains contain 10, 8, and 10 cysteine residues, respectively. The disulfide assignments of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ae0902cf90539b5679b512b4e15e611b
https://pubmed.ncbi.nlm.nih.gov/2250014
https://pubmed.ncbi.nlm.nih.gov/2250014