Cockroach Collagen: Isolation, Biochemical and Biophysical Characterization

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Abstract
Collagen fibrils from the mesenteric connective sheath of the adult cockroach P. americana were extracted by enzymatic digestion with pepsin and were purified. Chromatographic studies and sodium dodecyl sulfate electrophoresis revealed the presence of a single chain. The structure of this collagen could be represented by the formula (.alpha.)3. The amino acid composition is typical of collagens (1/3 glycine, and a high imino acid content) and similar to that of type II. The carbohydrate content was high (8.8%), and the cyanogen bromide pattern was different from that of known collagens. The chains were linked by the stable intermolecular bond dihydroxylysinonorleucine. The banding patterns of the segment-long-spacing crystallites and of the reconstituted fibrils were similar to type I collagen. The MW 280,000 and length (285 nm) were typical, but the denaturation temperature was high (38.5.degree. C). Cockroach mesenteric collagen showed the characteristic features of invertebrate mesodermal collagens, except that of the thermal stability of the triple-helical structure.