Section 8
Chapter 7,709

Purification and characterization of trehalase inhibitor from hemolymph of the American cockroach, Periplaneta americana

Hayakawa, Y.; Jahagirdar, A.P.; Yaguchi, M.; Downer, R.G.

Journal of Biological Chemistry 264(27): 16165-16169


ISSN/ISBN: 0021-9258
PMID: 2777784
Accession: 007708252

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An endogenous proteinaceous inhibitor of trehalase (.alpha.,.alpha.-trehalose-1-glucohydrolase: EC has been isolated and purified from the serum of resting adult American cockroaches, Periplaneta americana. Purification procedures involved decreasing ionic strength, gel filtration, and reversed phase high performance liquid chromatography. Homogeneity was confirmed by polyacrylamide gel electrophoresis and end group analysis. The purified protein inhibited trehalase activity in a dose-dependent manner and was estimated to have a molecular weight of 86,000 and to contain sugar chains. An automated gas-phase sequencer was used to determine the following sequence for the N-terminal amino acid residues: H-Ala-Ilu-Pro-Thr-Pro-His-Val-Tyr-Lys-Val-X-Val-Pro-Asp-Gly-Ala-Leu-Asn-Asp.

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