Isolation and Characterization of a Small Proteoglycan Associated with Porcine Intramuscular Connective Tissue

Abstract

In the present investigation, proteoglycan associated with porcine intramuscular collagen fibrils was isolated and characterized. The increase in the values of released uronic acid (percent) and heat solubility of collagen (percent) was observed by chondroitinase ABC digestion of intramuscular connective tissue isolated from porcine longissimus dorsi muscles, indicating that collagen fibril-associated proteoglycan was involved in the thermal stability of intramuscular collagen. A proteoglycan was purified from the adult porcine intramuscular connective tissue by successive steps of an extraction with 4 M guanidine hydrochloride, CsCl density gradient ultracentrifugation, DEAE-cellulose ion-exchange chromatography, and Sepharose CL-6B gel filtration. The isolated proteoglycan possessed an average molecular mass of 100 kDa and contained a core protein with mass of 48 kDa. Its constituent glycosaminoglycan chain was a dermatan sulfate, and the N-terminal amino acid sequence of its core protein was identical ...