Results 201 to 210 of about 265,113 (235)
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British Journal of Ophthalmology, 2022
Background/aims Nanophthalmos is a rare developmental, bilateral, sporadic or hereditary form of microphthalmos. In this study, the heterozygous variants c.781G>A and c.1066dup of the PRSS56 gene were identified in two patients with nanophthalmos.
Wei Wu +5 more
semanticscholar +3 more sources
Background/aims Nanophthalmos is a rare developmental, bilateral, sporadic or hereditary form of microphthalmos. In this study, the heterozygous variants c.781G>A and c.1066dup of the PRSS56 gene were identified in two patients with nanophthalmos.
Wei Wu +5 more
semanticscholar +3 more sources
Journal of the American Chemical Society, 2015
The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria.
L. Vieweg +8 more
semanticscholar +4 more sources
The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria.
L. Vieweg +8 more
semanticscholar +4 more sources
Role of a serine endopeptidase in the hydrolysis of exogenous cholecystokinin by brain slices.
Neuroscience, 1989The participation of a serine endopeptidase, previously shown to be involved in endogenous cholecystokinin inactivation [Rose, Camus and Schwartz (1989) Neuroscience 29, 583-594], in the hydrolysis of various exogenous cholecystokinin peptides was studied with slices from rat cerebral cortex.
A. Camus, C. Rose, J. Schwartz
semanticscholar +3 more sources
Serine Endopeptidase Activities of Cowpea Seeds: A Time Course during Development and Germination
Crop Science, 2019ABSTRACTProteases in plants carry out an essential role in protein turnover during seed development and germination. Cysteine proteases (EC 3.4.22) are well‐known participants of such processes. Serine proteases (EC 3.4.21), however, are far less reported as protagonists during these events.
N. B. Lima +6 more
semanticscholar +2 more sources
Improved isolation, stability and substrate specificity of cucumisin, a plant serine endopeptidase
Biotechnology and Applied Biochemistry, 1995Cucumisin (EC 3.4.21.25), a serine endopeptidase, was isolated by a simple purification procedure from the prince melon (Cucumis melo ssp. melo, cv. ‘Prince Melon’).
M. Kaneda, H. Yonezawa, T. Uchikoba
semanticscholar +3 more sources
Biological Chemistry, 2017
AbstractAeromonas sobriaserine protease (ASP) is secreted fromAeromonas sobria, a pathogen causing gastroenteritis and sepsis. ASP resemblesSaccharomyces cerevisiaeKex2, a member of the subtilisin family, and preferentially cleaves peptide bonds at the C-terminal side of paired basic amino acid residues; also accepting unpaired arginine at the P1site ...
T. Imamura, Y. Murakami, H. Nitta
semanticscholar +3 more sources
AbstractAeromonas sobriaserine protease (ASP) is secreted fromAeromonas sobria, a pathogen causing gastroenteritis and sepsis. ASP resemblesSaccharomyces cerevisiaeKex2, a member of the subtilisin family, and preferentially cleaves peptide bonds at the C-terminal side of paired basic amino acid residues; also accepting unpaired arginine at the P1site ...
T. Imamura, Y. Murakami, H. Nitta
semanticscholar +3 more sources
Partial purification and characterization of a serine endopeptidase from rat liver plasma membranes
Biochimica Et Biophysica Acta - General Subjects, 1986A serine endopeptidase was partially purified from rat liver plasma membranes by using a four-step procedure: solubilization with N-lauroylsarcosine; Ultrogel AcA-34 chromatography; CM Affi-Gel blue chromatography; agarose-soybean trypsin inhibitor chromatography.
L, Guenet +4 more
exaly +3 more sources
Canadian Journal of Microbiology, 2002
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C. H. De Toni +4 more
semanticscholar +3 more sources
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C. H. De Toni +4 more
semanticscholar +3 more sources
Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases
Biochemical and Biophysical Research Communications, 1988Yeast Saccharomyces cerevisiae KEX2 gene previously isolated, was characterized as the gene encoding a calcium-dependent endopeptidase required for processing of precursors of alpha-factor and killer toxin. In this study, we report the amino acid sequence of the KEX2 gene product deduced from nucleotide sequencing.
Kensaku Mizuno
exaly +3 more sources