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

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TypeArticle
Journal titleThe Journal of Biological Chemistry
Volume264
Issue27
Pages1616516169; # of pages: 5
AbstractAn endogenous proteinaceous inhibitor of trehalase (alpha,alpha-trehalose-1-glucohydrolase: EC 3.2.1.28) 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-Le u-Asn-Asp.
Publication date
Linkhttp://www.jbc.org/content/264/27/16165.full.pdf
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedNo
NRC numberHAYAKAWA1989
NPARC number9364137
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Record identifier73d24ca6-5b46-40a4-8b61-9f75a5a37b1f
Record created2009-07-10
Record modified2016-05-09
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