Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C1389183 (
autodigestion
)
317
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Alkaline metalloendopeptidase (metalloprotease)
AP1
(48 kDa) from Vibrio sp. isolated from the intestine of a five-barred goatfish (Parupeneus trifasciatus) was reported in our previous paper to produce AP2 (36 kDa) by releasing a peptide fragment (molecular mass of about 12 kDa) from the C-terminal end of
AP1
by
autodigestion
.
AP1
strongly agglutinated fish (flounder, Paralichthys olivaceus) and rabbit erythrocytes, and weakly chicken erythrocytes. In contrast, AP2 had no significant hemagglutinating activity toward any erythrocytes tested, except for weak activity on flounder erythrocytes, suggesting that the C-terminal region of
AP1
may be required for the strong hemagglutinating activity. The optimum temperature for the hemagglutinating activity of
AP1
was found to be lower than that for the proteolytic activity. At acidic pHs (below pH 7.5), the hemagglutinating activity of
AP1
decreased, and its pH profile resembled that of the proteolytic activity. The hemagglutinating activity of
AP1
was not observed in the presence of o-phenanthroline or synthetic and proteinous substrates, but different kinds of saccharides and lipids had no effect. While the proteolytic activity of
AP1
was not affected by CaCl2, the hemagglutinating activity of
AP1
decreased with increases in CaCl2 concentrations. These results suggested that the hemagglutinating activity of these proteases (
AP1
and AP2) was most likely caused by their proteolytic action on erythrocyte cell surfaces.
...
PMID:Hemagglutinating activity of extracellular alkaline metalloendopeptidases from Vibrio sp. NUF-BPP1. 969 99
