The Chromatographic Separation and Amino Acid Composition of the Subunits of Several Collagens^*

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

“…Type I collagen was prepared in the laboratory from Sprague Dawley rat (Depre, St. Doulchard, France) tail tendons by 0.5 M acetic acid extraction (9) and used as native acid-soluble collagen or after pepsin digestion to remove telopeptides (10). Type I acid-soluble and pepsinized collagens used in this study were denatured by heating at 60°C for 30 min.…”

Isolation and characterization of two collagenous components from anterior lens capsule

“…The fractions obtained from Bio-Gel A-5 M columns were purified by carboxymethyl cellulose chromatography [11,14]. Recoveries from molecular sieve and carboxymethyl cellulose columns were 70-80% and 40-50%, respectively.…”

Different antigenic determinants in the polypeptide chains of human collagen

“…Subsequently the acid-soluble collagen was extracted either by 0.05 M citrate buffer pH 3.7 or 1% acetic acid and was purified by two precipitations with KC1 [8]. The a-chains were separated by CM-cellulose chromatography [9] and the ct2-chains further purified by molecular sieve chromatography [10]. Since the yields of acid-soluble collagen from human tissues are very low, the cyanogen bromide peptides (CB-peptides) were prepared from the insoluble collagen not dissolved by the extractions described above.…”