Collagen polymorphism: characterization of molecules with the chain composition (alpha 1 (3)03 in human tissues.
Collagen moleculess with the chain comizposition [alpha1(III)](3), have been isolated from pepsin-solubilized collagen of dermis, aorta, and leiomlyoma of the uterus by differential salt precipitation. On denaturation, approximately 90 percent of this collagen is recovered as a gamma component (300,000 daltons). Reduction and alkylation of the high-molecular-weight component yields alpha1(III) chains (95,000 daltons). In addition to containing cysteine, alpha1(III) chains exhibit several other compositional differences when compared to alpha1(I), alpha1(II), or alpha2 chains from human tissues.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001013:Aorta, Thoracic / Q000032:analysis; D001322:Autoanalysis; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000032:analysis* / Q000096:biosynthesis; D005260:Female; D006801:Humans; D007231:Infant, Newborn; D007889:Leiomyoma; D008970:Molecular Weight; D011110:Polymorphism, Genetic; D012867:Skin / Q000032:analysis; D014594:Uterine Neoplasms
D000596:Amino Acids; D003094:Collagen