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GrainGenes Reference Report: JFC-42-2382

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Reference
JFC-42-2382
Title
Purification and characterization of proteinous inhibitor of lipase from wheat flour
Journal
Journal of Agricultural and Food Chemistry
Year
1994
Volume
42
Pages
2382-2385
Author
Tani H
Ohishi H
Watanabe K
Abstract
Proteinous lipase inhibitor (LI) from wheat flour was purified to homogeneity using hydrophobic chromatography, gel chromatography, affinity chromatography, SDS-PAGE, and two-dimensional electrophoresis Molecular masses of the LIs were approximately 28 and 25 kDa as estimated by SDS-PAGE The amino acid sequences from the N termini of the three components detected by two-dimensional electrophoresis were Arg-Ser-Ala-His-Glu-Pro-Gln-Gln-Pro in the two 25 kDa isolates and Arg-Ser-Ala-His-Glu-Glu-Gln-Gln-His in the 28 kDa isolate, and they were suggested to be genetic variants The LI was activated by the heating procedure up to 80 degrees C and stable in the pH range from 3.0 to 7.0. Porcine pancreatic lipase was inhibited through direct interaction with LI, while the activity for the lipase from Candida cylindracea was partially inhibited and those of the other microbacteria were not inhibited.
Keyword
amino acid sequence
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