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N-terminal Sequence of a Core Protein From a Biglycan Isolated From Bovine Aorta

N-terminal Sequence of a Core Protein From a Biglycan Isolated From Bovine Aorta

X L Zhu, B Radhakrishnamurthy, J H Xu, S R Srinivasan, G S Berenson

Connect Tissue Res. 1995;31(2):125-32.

PMID: 15612328

Abstract:

A biglycan was isolated from bovine aorta intima media by 4M guanidine HCl extraction of the tissue; the material was fractionated and purified by using isopycnic ultracentrifugation and DEAE Sephacel ion-exchange chromatography. Core proteins, resulting from digestion of the proteoglycan preparation with chondroitinase ABC, were resolved by SDS-polyacrylamide gel electrophoresis into three bands. The apparent molecular weight of the fast migrating major protein band was 47 kDa and the other slow-moving minor protein bands were 90 and 105 kDa. These proteins were recognized by a monoclonal anti-proteoglycan deltaDi-6S (MAb 3-B-3/Cl). The amino acid composition of 47 kDa core protein revealed a high content of aspartic acid, glutamic acid and leucine, similar to those found for biglycans isolated from bovine cartilage, rat vascular smooth muscle cell culture and human bone. The N-terminal sequence of 47 kDa core protein was determined as Asp-Glu-Glu-Ala-X-Gly-Ala-Glu-Thr-Thr-X-Gly-Ile-Pro-Asp which is identical to the sequence of bovine articular cartilage biglycan. The proteoglycan had two glycosaminoglycan chains.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241138	Biglycan from bovine articular cartilage			Price

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