Monomeric alkaline phosphatase of Vibrio cholerae.

نویسندگان

  • N K Roy
  • R K Ghosh
  • J Das
چکیده

Alkaline phosphatase has been purified to homogeneity from two strains of Vibrio cholerae. The enzymes from both strains are single polypeptides of molecular weight 60,000. Both of the enzymes have pH optima around 8.0 and can act on a variety of organic phosphate esters, glucose-1-phosphate being the best substrate. The enzymes are unable to hydrolyze ATP and AMP. Although they have identical Km values, the two enzymes differ significantly in Vmax with p-nitrophenyl phosphate as substrate. The enzymes from the two strains also differ in their sensitivity to EDTA, Pi, and metal ions and activities of the apoenzymes. Ca2+ reactivated the apoenzymes most.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Sialidase from different sources compared for electrophoretically separating serum alkaline phosphatase fractions from liver and bone.

We compared sialidase (neuraminidase; EC 3.2.1.18) from Vibrio cholerae, Clostridium perfringens, and Arthrobacter ureafaciens, seeking to improve the electrophoretic separation of the liver and bone isoenzymes of alkaline phosphatase (EC 3.1.3.1) on cellulose acetate membranes. Resolution is decisively determined by the type and activity of sialidase used in the preincubation of serum sample. ...

متن کامل

Development and testing of a nonradioactive DNA oligonucleotide probe that is specific for Vibrio cholerae cholera toxin.

An alkaline phosphatase-labeled oligonucleotide DNA probe (CTAP) that was specific for the cholera toxin gene (ctxA) was identified. All cholera toxin-producing strains of Vibrio cholerae, regardless of serotype, hybridized with the CTAP probe, while nontoxigenic strains from either environmental sources or from deletion or substitution mutations did not hybridize. Unlike the whole-gene probes ...

متن کامل

Repression of the alkaline phosphatase of Vibrio cholerae.

The synthesis of alkaline phosphatase by two strains of Vibrio cholerae belonging to the Inaba and Ogawa serotypes has been examined in relation to the phosphate concentration of the culture medium. The synthesis of the enzyme in both strains was repressed in cells grown in the presence of a high concentration of inorganic phosphate. Lowering the phosphate content of the growth medium led to a ...

متن کامل

Polyphosphate stores enhance the ability of Vibrio cholerae to overcome environmental stresses in a low-phosphate environment.

Vibrio cholerae, the causative agent of Asiatic cholera, has been reported to make large quantities of polyphosphate. Inorganic polyphosphate is a ubiquitous molecule with a variety of functions in prokaryotic and eukaryotic cells. We constructed a V. cholerae mutant with a deletion in the polyphosphate kinase (ppk) gene. The mutant was defective in polyphosphate biosynthesis. Deletion of ppk h...

متن کامل

Occurrence of Pathogenic Vibrios in Coastal Areas of Golestan Province in Iran

  This study was carried out to investigate the occurrence of potentially pathogenic species of vibrio in sea water and estuarine environments of the Caspian Sea in the Golestan province of Iran. A total of 127 water samples from coastal waters as well as from river and estuaries were collected and analyzed by culture, during April and September 2001. Following prompt centrifugation, the resusp...

متن کامل

ذخیره در منابع من

ذخیره در منابع من قبلا به منابع من ذحیره شده

{@ msg_add @}


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Journal of bacteriology

دوره 150 3  شماره 

صفحات  -

تاریخ انتشار 1982