[Isolation and properties of a preparation of arterial collagen solubilized by pretreatment with alkali (author's transl)].
The acid-soluble, highly cross-linked aorta collagen, of which about 30% can be converted into a soluble form by alkali treatment, followed by extraction with aetic acid, was obtained predominantly in the form of monomeric, helical molecules, as indicated by the value for the intrinsic viscosity and its behaviour in sodium dodecylsulphate disc electrophoresis. Apart from decreased values for tyrosine (0.26%), arginine (4.4%) and aspartic acid (3.9%), the amino acid composition of the aorta collagen fraction was similar to that of the acid-soluble calf skin collagen. This finding, together with the cyanogen bromide peptide pattern, shows that the collagen extracted from the artery is predominantly type I. Treatment with alkali probably shortens the alpha1-CB6-peptide by about 45 amino acids. The collagen extracted from artery was compared with acid soluble skin collagen by sodium dodecylsulphate polyacrylamide electrophoresis. The arterial collagen showed a marked increase in the rations alpha1 to alpha2 (4:1), alpha to beta (3:1) and beta11 to beta12 (2.5:1). Compared with acid soluble skin collagen, the aorta collagen contained twice as much galactose and glucose (13.5 and 9.6 nmol/mg protein respectively), which are bound to hydroxylysine. 50% of the hydroxylysine residues are unsubstituted, 15% are present as galactosyl hydroxylysine, and 35% as glucosyl-galactosyl hydroxylysine. On the basis of its reported properties, arterial collagen obtained by the method of Fujii appears to be a suitable substrate for the study of the enzymic synthesis and enzymic degradation of hydroxylysine glycosides of native arterial collagen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis*; D002417:Cattle; D003094:Collagen / Q000302:isolation & purification*; D003720:Densitometry; D004589:Electrophoresis, Disc; D005690:Galactose / Q000032:analysis; D005947:Glucose / Q000032:analysis; D006868:Hydrolysis; D006901:Hydroxylysine / Q000302:isolation & purification; D011487:Protein Conformation; D012867:Skin / Q000032:analysis; D012995:Solubility; D014783:Viscosity
D000596:Amino Acids; D006901:Hydroxylysine; D003094:Collagen; D005947:Glucose; D005690:Galactose
Isolierung und Eigenschaften eines nach Alkali-Vorbehandlung Iöslichen Arterienkollagens