Results 171 to 180 of about 16,013 (203)

In Silico Analysis of C₆₀ Fullerene Interaction with TMPRSS2: Toward Novel COVID-19 Prevention Approaches. [PDF]

Molecules
Hurmach V, Karaushu V, Prylutska S, Klestova Z, Vyzhva S, Prylutskyy Y, Ritter U, Garamus V.   +7 more
europepmc   +1 more source

Staphylococcus aureus SspA (V8 protease): New skin pathogenesis insights into an old enzyme. [PDF]

PLoS Pathog
Thorstenson JC, Horswill AR.
europepmc   +1 more source

Cysteine proteases and how YabG fits into clan CD of the MEROPS database. [PDF]

J Bacteriol
Osborne MS, Sorg JA.
europepmc   +1 more source

Comparative characterization of two serine endopeptidases from Nocardiopsis sp. NCIM 5124

Biochimica et Biophysica Acta (BBA) - General Subjects, 2000
A protease-producing, crude oil degrading marine isolate was identified as Nocardiopsis sp. on the basis of the morphology, cell wall composition, mycolic acid analysis and DNA base composition. The Nocardiopsis produces two extracellular proteases, both of which are alkaline serine endopeptidases.
V S, Dixit, A, Pant
openaire   +3 more sources

[10] IgA-specific prolyl endopeptidases: Serine type

, 1994
Andrew G. Plaut, William W. Bachovchin
openaire   +2 more sources

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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
openaire   +2 more sources

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
openaire   +2 more sources

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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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