Results 161 to 170 of about 122,475 (202)

Specificity comparison of a serine endopeptidase (SH1) and a serine thiol endopeptidase (STH2) purified from human urine

The International Journal of Biochemistry & Cell Biology, 2004
In this study, we compared the properties of a serine endopeptidase H1 (SH1) and a serine thiol endopeptidase (STH2) purified from human urine by DEAE-cellulose followed by a Bio Gel A0.5 m or Sepharose Mercurial chromatographs. These enzymes differ in their action upon different hormone peptides.
B M R, Quinto, M A, Juliano, I, Hirata, A K, Carmona, L, Juliano, D E, Casarini   +5 more
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A serine endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim.

Phytochemistry, 2001
An endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim. has been purified by DEAE-Sepharose chromatography and gel-filtration by a Sephacryl S-300. The enzyme has Mr of 61 kDa. The optimum pH of the enzyme was 8. The enzyme activity was inhibited by diisopropyl fluorophosphate and phenylmethanesulfonylfluoride, but not by EDTA.
T, Uchikoba, S, Hosoyamada, M, Onjyo, K, Arima, H, Yonezawa, M, Kaneda   +5 more
openaire   +2 more sources

Role of a serine endopeptidase in the hydrolysis of exogenous cholecystokinin by brain slices

Neuroscience, 1989
The 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 C, Schwartz
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Polyproline fold—In imparting kinetic stability to an alkaline serine endopeptidase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
Polyproline II (PPII) fold, an unusual structural element was detected in the serine protease from Nocardiopsis sp. NCIM 5124 (NprotI) based on far UV circular dichroism spectrum, structural transitions of the enzyme in presence of GdnHCl and a distinct isodichroic point in chemical and thermal denaturation.
Sonali B, Rohamare, Vaishali, Dixit, Pavan Kumar, Nareddy, D, Sivaramakrishna, Musti J, Swamy, Sushama M, Gaikwad   +5 more
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Improved isolation, stability and substrate specificity of cucumisin, a plant serine endopeptidase

Biotechnology and Applied Biochemistry, 1995
Cucumisin (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’). The enzyme is stable over a wide pH range (4‐11) and to heat, 80% of its initial activity remaining even at pH 11.1 and at 60 degrees C for 20 min.
M, Kaneda, H, Yonezawa, T, Uchikoba
openaire   +2 more sources

Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases

Biochemical and Biophysical Research Communications, 1988
Yeast 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.
K, Mizuno, T, Nakamura, T, Ohshima, S, Tanaka, H, Matsuo   +4 more
openaire   +2 more sources

Partial purification and characterization of a serine endopeptidase from rat liver plasma membranes

Biochimica et Biophysica Acta (BBA) - General Subjects, 1986
A 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, F, Gueble-Val, M, Blayau, A, Le Treut, J Y, Le Gall   +4 more
openaire   +2 more sources

Heterozygous variants c.781G>A and c.1066dup ofserine protease 56cause familial nanophthalmos by impairing serine-type endopeptidase activity

British Journal of Ophthalmology, 2022
Background/aimsNanophthalmos is a rare developmental, bilateral, sporadic or hereditary form of microphthalmos. In this study, the heterozygous variants c.781G>A and c.1066dup of thePRSS56gene were identified in two patients with nanophthalmos. This study reports the clinical manifestation and the underlying pathogenic mechanism.MethodsWhole-exome ...
Wei Wu, Jingjie Xu, Houfa Yin, Chenxi Fu, Ke Yao, Xiangjun Chen   +5 more
openaire   +2 more sources

Further Characterization of Endopeptidase H2 a Serine Proteinase from Human Urine

1992
A human urine serine proteinase chymotrypsin like hydrolyzes the peptide bonds: Phe-Ser (kinin); Gly-Gly, Leu-Arg, Phe-Lys (neuropeptides) and Gln-Gln (substance P). Endopeptidase H2 hydrolyzes better oligopeptides with 4 to 18 aminoacid residues than larger peptides, it does not hydrolyzes kininogen or proenkephalin.
D E, Casarini, C E, Fellows, R C, Stella, C A, Sampaio   +3 more
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The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides

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.
Vieweg, Laura, Kretz, Julian, Pesic, Alexander, Kerwat, Dennis, Grätz, Stefan, Royer, Monique, Cociancich, Stéphane, Mainz, Andi, Süssmuth, Roderich   +8 more
openaire   +3 more sources