Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The 987P fimbriae of enterotoxigenic Escherichia coli (ETEC) mediates adhesive interactions with brush border vesicle (BBV) of the intestinal epithelial cells from the neonatal piglets. By adhering to intestinal epithelial cells, producing localized multiplication, the 987P ETEC can progress to mucosal surface colonization and concomitant effective enterotoxin delivery. To identify the receptors for the 987P, BBV proteins from piglet intestinal villous epithelial cells were separated by SDS-PAGE and analyzed by Ligand blot, protein bands with a set of 32-35 kD recognized by the 987P fimbriae were subjected to in gel proteolysis with trypsin. The tryptic fragments were separated by microbore reversed phase HPLC(RP-HPLC), samples shown to contain one major peak by MALDI-MS were submitted to Edman sequencing, three peptides were sequenced successfully and the all of three peptides matched the sequences of human or porcine histone H1 proteins. Porcine histone H1 proteins isolated from both piglet intestinal epithelial cells and BBV demonstrated the same SDS-PAGE migration pattern and 987P-binding properties as the 987P-specific protein receptors from piglet intestinal brush border did. The above results indicated that the 987P protein receptors are piglet BBV-derived Histone H1 proteins.
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PMID:[Identification of the 987P protein receptors for enterotoxigenic Escherichia coli]. 1858 9

Linker Histone-Like proteins (LHL1 and LHL2) were identified within a linker histone complement of Muscovy duck erythrocyte chromatin. Polyacrylamide gel electrophoretic patterns of N-bromosuccinimide-cleaved LHL products as well as liquid chromatography-electrospray-ion trap mass spectrometry analyses of trypsin-digested LHL peptides revealed structural similarity of LHL1 to histone H5 and between LHL2 and histone H1 subtypes. Since the LHL proteins were stable in the presence of 2-mercaptoethanol and dithiothreitol that reduce disulfide bonds, it appeared unlikely that this doublet was a thiol-derived product of linker histones. A loss of LHL1, with a concomitant maintenance of LHL2 after treatment with dilute alkali, seems to suggest that they might represent disparate protein conjugates resulting from linker histone modifications through ester linkages.
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PMID:Linker histone-like proteins in Muscovy duck (Cairina moschata L) erythrocyte chromatin. 1938 32


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