Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study identifies the in vitro differences (markers) between virulent and attenuated transmissible gastroenteritis (TGE) viruses. Exposure of virulent Miller strain and attenuated Purdue strain TGE viruses to a spectrum of acidities indicated that the Miller strain was more stable at pH 2. Acidities at or above pH 3 did not reduce viral infectivity of either strain. When virulent and attenuated viruses were exposed to gastric fluids of either fed or fasted swine, there was a similar degree of sensitivity. Carboxypeptidase B, alpha-amylase, and alkaline phosphatase present in porcine small intestinal fluids did not cause a significant difference in sensitivity between virulent and attenuated virus isolates. The digestive enzymes: trypsin, alpha-chymotrypsin, pancreatin, peptidase, and carboxypeptidase A did not (or only slightly) inactivate virulent Miller strain TGE virus, but greatly reduced infectivity of attenuated viruses (Purdue strain and TGE vaccine virus isolates). The attenuated strains were significantly more sensitive to small intestinal fluids from both fasted and fed adult swine. Differential sensitivities between virulent and attenuated TGE viruses to digestive fluids from stomach and small intestine further substantiate the notion of differential susceptibility to small intestinal proteases as a correlate of viral virulence.
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PMID:Enzymatic and acidic sensitivity profiles of selected virulent and attenuated transmissible gastroenteritis viruses of swine. 298 96

The detergents, sodium dodecyl sulfate (SDS), lauryl glutamate (LG), and octyl-(polydisperse)oligooxyethylene (Octyl-POE), were tested as to their effects on the activities of carboxypeptidases A, B, and P. In general, Octyl-POE showed little inhibition and SDS showed the strongest inhibition. Carboxypeptidase B was only slightly inhibited by SDS. The inhibitory effect of SDS on these enzyme activities depended not on its concentration but on its absolute amount. For a constant amount of SDS, the activities of carboxypeptidases A and B remained almost constant with increasing reaction volume. Commercial carboxypeptidase B is usually contaminated by carboxypeptidase A. With the addition of SDS, almost only carboxypeptidase B activity was detected.
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PMID:Carboxypeptidase digestion in the presence of detergents. 366 69