The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage.
作者： P.J. Neame , R.E. Boynton , Y. Sommarin , D. Heinegård
DOI: 10.1016/S0021-9258(17)31839-2
关键词:
摘要: A leucine-rich protein, chondroadherin, has been isolated from dissociative extracts of articular cartilage, and its primary structure determined by both direct protein sequencing DNA sequence analysis polymerase chain reaction products cDNA clones. This is identical to the 36-kDa which was Larsson et al. (Larsson, T., Sommarin, Y., Paulsson, M., Antonsson, P., Hedbom, E., Wendel, Heinegard, D. (1991) J. Biol. Chem. 266, 20428-20433). It 337 amino acids exists in several isoforms. The two major isoforms are a form with calculated molecular weight 38,353 pI 9.76 smaller 37,304 9.5. result cleavage near C terminus. further level heterogeneity found that an extra alanine can be prior N-terminal cysteine. There 9 cysteines; disulfide bonds have directly identified between Cys282-Cys324 Cys284-Cys304. principal feature series 10 repeats. most these repeats contains cysteine (Cys63) not disulfide-bonded difficult derivatize. likely this free involved structure-stabilizing hydrogen bonding. mRNA approximately 1.6 kilobases, 511 base pairs 3‘-untranslated region stop codon polyadenylation signal. Based on anchored mRNA, there some minor position 5‘ end message.
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