期刊论文详细信息
FEBS Letters | |
Modification of the laminin α4 chain by chondroitin sulfate attachment to its N‐terminal domain | |
Mann, Karlheinz1  Sasaki, Takako1  Timpl, Rupert1  | |
[1] Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany | |
关键词: Basement membrane; Laminin; Proteoglycan; Tissue expression; | |
DOI : 10.1016/S0014-5793(01)02812-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The N-terminal domain of laminin α4 chains corresponds to a short rod-like structure which after recombinant production was found to be modified by chondroitin sulfate. Substitution occurred mainly to a single serine in its N-terminal ASGDG sequence. A similar yet partial modification was also demonstrated for the α4 chain present in extracts of adult mouse tissues. Antibodies to the fragment were useful to demonstrate a relatively high content of α4 in several tissues and for the immunolocalization in various blood vessels, some basement membranes and interstitial regions.
【 授权许可】
Unknown
【 预 览 】
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