Literature DB >> 7981662

Inhibition of prophenoloxidase-activating enzyme from Bombyx mori by endogenous chymotrypsin inhibitors.

Y Aso1, T Yamashita, K Meno, M Murakami.   

Abstract

Inhibitory activities for the activation of prophenoloxidase with its activating enzyme were detected in the gel-filtration fractions of hemolymph from Bombyx mori. The fractions with the highest activity contained chymotrypsin inhibitors; CI-13a, 13b, and 13c. They inhibited the activation of prophenoloxidase. The activating enzyme affected a synthetic substrate for trypsin, Boc-Gln-Ala-Arg-MCA: Km = 0.62 mM. CI-13c partially suppressed the peptidase activity.

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Year:  1994        PMID： 7981662

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN： 1039-9712


  3 in total

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Authors:  André N Pitaluga; Vicente Beteille; Amanda R Lobo; João R Ortigão-Farias; Alberto M R Dávila; Adelson A Souza; J Marcelo Ramalho-Ortigão; Yara M Traub-Cseko
Journal:  Mol Genet Genomics       Date:  2009-06-30       Impact factor: 3.291

2.  KPI5 Is Involved in the Regulation of the Expression of Antibacterial Peptide Genes and Hemolymph Melanization in the Silkworm, Bombyx mori.

Authors:  Jingya Heng; Huawei Liu; Jiahui Xu; Xuan Huang; Xiaotong Sun; Runze Yang; Qingyou Xia; Ping Zhao
Journal:  Front Immunol       Date:  2022-05-20       Impact factor: 8.786

3.  Genome-wide identification and immune response analysis of serine protease inhibitor genes in the silkworm, Bombyx mori.

Authors:  Ping Zhao; Zhaoming Dong; Jun Duan; Genhong Wang; Lingyan Wang; Youshan Li; Zhonghuai Xiang; Qingyou Xia
Journal:  PLoS One       Date:  2012-02-13       Impact factor: 3.240
  3 in total

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