Serine protease from midgut of Bombus terrestris males

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00391467" target="_blank" >RIV/61388963:_____/13:00391467 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/13:00391467

Výsledek na webu

<a href="http://dx.doi.org/10.1002/arch.21075" target="_blank" >http://dx.doi.org/10.1002/arch.21075</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/arch.21075" target="_blank" >10.1002/arch.21075</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Serine protease from midgut of Bombus terrestris males

Popis výsledku v původním jazyce

A serine protease was isolated from midguts of the bumblebee male Bombus terrestris by a combination of precipitation procedures with column chromatography. The purified enzyme exhibited two bands with molecular masses of 25 and 26 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These bands showed a proteolytic activity in zymography assay. Midgut enzymes showed optimum proteolytic activity at pH 9 and 35 degrees C using N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenyl-alanine 4-nitroanilide as a substrate. The Michaelis constant (Km) and maximum reaction rate (Vmax) were 0.55 +/- 0.042 mM and 0.714 +/- 0.056 mol p-nitroalanine produced min1 mg protein1, respectively. Inhibition was affected by trypsin inhibitor, but not by phenylmethylsulfonyl fluoride and N-tosyl-L-phenylalanine chloromethyl ketone, which indicated the trypsin-like but not chymotrypsin-like specificity. The identity of the serine protease was confirmed by nanoliquid-tandem mass spectrome

Název v anglickém jazyce

Serine protease from midgut of Bombus terrestris males

Popis výsledku anglicky

A serine protease was isolated from midguts of the bumblebee male Bombus terrestris by a combination of precipitation procedures with column chromatography. The purified enzyme exhibited two bands with molecular masses of 25 and 26 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These bands showed a proteolytic activity in zymography assay. Midgut enzymes showed optimum proteolytic activity at pH 9 and 35 degrees C using N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenyl-alanine 4-nitroanilide as a substrate. The Michaelis constant (Km) and maximum reaction rate (Vmax) were 0.55 +/- 0.042 mM and 0.714 +/- 0.056 mol p-nitroalanine produced min1 mg protein1, respectively. Inhibition was affected by trypsin inhibitor, but not by phenylmethylsulfonyl fluoride and N-tosyl-L-phenylalanine chloromethyl ketone, which indicated the trypsin-like but not chymotrypsin-like specificity. The identity of the serine protease was confirmed by nanoliquid-tandem mass spectrome

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Archives of Insect Biochemistry and Physiology

ISSN

0739-4462

e-ISSN

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Svazek periodika

82

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

117-128

Kód UT WoS článku

000315102100002

EID výsledku v databázi Scopus

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