| Literature DB >> 8117283 |
R Kobayashi1, A Mizutani, H Hidaka.
Abstract
We have reported here the biochemical characterization of a newly identified microfibril-associated protein of 36-kDa (36-kDa MAP) from bovine aorta. Using Ca(2+)-dependent affinity chromatography on an isoquinolinesulfonamide derivative (CKA-1303)-coupled Sepharose, we obtained a pure form of 36-kDa MAP. This compound should serve as a useful tool for clarifying the physiological roles of 36-kDa MAP. In addition, 45Ca-autoradiography clearly indicated that 36-kDa MAP binds Ca2+. Partial amino acid sequence of 36-kDa MAP was determined. Our search of that published sequence against a 36-kDa MAP sequence revealed the resemblance to fibrinogen-related proteins of sea cucumber, cytotactin and tenascin which are substrate-adhesion proteins made at critical stages of histogenesis.Entities:
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Year: 1994 PMID: 8117283 DOI: 10.1006/bbrc.1994.1178
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575