Abstract:
:Cucumisin was isolated from prince melon sarcocarp by means of a simple purification procedure. Serine protease inhibitors such as soybean trypsin inhibitor, ovomucoid, and aprotinin had no effect on the enzyme activity. alpha 2-Macroglobulin showed 38% inhibition of the original caseinolytic activity of cucumisin. The favorable synthetic substrates for cucumisin were Glt-Ala-Ala-Pro-Leu-pNA and Suc-Ala-Ala-Pro-Phe-pNA. The constant (kcat/Km) for Suc-Ala-Pro-Ala-pNA was found to be 30 times greater than that for Suc-Ala-Ala-Ala-pNA. The substrate specificity of cucumisin for oligopeptides and proteins was shown to be broad.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Uchikoba T,Yonezawa H,Kaneda Mdoi
10.1093/oxfordjournals.jbchem.a124817subject
Has Abstractpub_date
1995-05-01 00:00:00pages
1126-30issue
5eissn
0021-924Xissn
1756-2651journal_volume
117pub_type
杂志文章abstract::The mitogen-activated protein kinase (MAPK) signaling pathway, which is conserved from yeast to humans, is activated in response to a variety of extra- and intracellular stimuli, and plays key roles in multiple cellular processes, including proliferation, differentiation, and apoptosis. The MAPK pathway transmits its ...
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journal_title:Journal of biochemistry
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