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: EC:3.4.21.4 (
trypsin
)
42,187
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with
trypsin
, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514.
Protein II
had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.
...
PMID:The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus. 642 Jan 94
One molecule of UTI68, a trypsin inhibitor purified from urine of healthy men, inhibited four molecules of bovine
trypsin
. This finding suggests the formation of various complexes of UTI68 with 1 to 4 molecules of
trypsin
. However, SDS polyacrylamide gel electrophoresis of the reaction products of UTI68 with
trypsin
showed that, at molecular ratios of UTI68 to
trypsin
of 1:1 to 1:3, UTI68 was rapidly cleaved by
trypsin
to form two proteins, Protein I and
Protein II
, whose molecular weights were estimated as 49,000 and 25,000, respectively, while at a ratio of 1:4, UTI68 was converted to Protein III with a molecular weight of about 30,000 and a smaller protein(s) than
trypsin
. These results were supported by gel filtration of the reaction products of UTI68 with
trypsin
on a Sephadex G-100 column at pH 3.0. Protein I and
Protein II
were separated, and Protein I was named UTI49.
Protein II
was separated from
trypsin
on a QAE-Sephadex column, and it had no inhibitory activity. Since one molecule of UTI49 inhibited about three molecules of
trypsin
, its interaction with
trypsin
was examined. On addition of one and two molecules of
trypsin
to one molecule of UTI49 at pH 8.0 complexes were formed consisting of one and two molecules of
trypsin
, respectively, with one molecule of UTI49, and both complexes were dissociated to their components at pH 3.0. Addition of three molecules of
trypsin
brought about further fragmentation of UTI49, and the split products formed a complex(es) with
trypsin
at pH 8.0, which dissociated at pH 3.0.
...
PMID:Interaction of urinary trypsin inhibitor, UTI68, with bovine trypsin. 709 94
