Structural analysis of the extension peptides on matrix forms of type V collagen in fetal calf bone and skin.
The structure of the extension peptides retained on the tissue form of type V collagen molecules was determined. Type V collagen alpha chains containing extension peptides were extracted from fetal calf skin and bone by 4 M guanidine-HCl and 0.5 M acetic acid, respectively. Collagens present in both extracts were fractionated by sodium chloride precipitation. The collagen alpha(V) chains were then resolved by reverse-phase high performance liquid chromatography. The N-terminal extension peptides were characterized by direct sequence analysis after deblocking with pyroglutamate amino-peptidase and analysis of the products of digestion by bacterial collagenase, chymotrypsin, V8 protease and endoproteinase Lys-C. The results showed that the retained extension peptides on type V collagen molecules in the extracellular matrix of skin and bone were amino-propeptides and that the alpha 2(V) chain retains an intact amino-propeptide while the alpha 1(V) chain appears to be partially processed. The extended alpha 1(V) chain isolated from fetal calf bone gave an identical amino-terminal sequence to that of the alpha 1(V) chain isolated from fetal calf skin, suggesting that a specific enzyme may be involved in processing the alpha 1(V) amino-propeptide.
Niyibizi
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Department of Orthopaedics, University of Washington, Seattle 98195.
Eyre
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D000595:Amino Acid Sequence; D000818:Animals; D001842:Bone and Bones / Q000737:chemistry*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D012867:Skin / Q000737:chemistry*
D010455:Peptides; D003094:Collagen