Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Arylsulfatase from Pseudomonas sp. strain C12B: purification to homogeneity, immunological analysis, and physical properties.

Literature DB >> 7204346

Arylsulfatase from Pseudomonas sp. strain C12B: purification to homogeneity, immunological analysis, and physical properties.

Abstract

Arylsulfatase was purified 219-fold from Pseudomonas sp. strain C12B. The final preparation was homogeneous by electrophoretic and immunological analysis. The enzyme is a monomer of molecular weight about 51,000, with a Stokes radius of 3.0 X 10(-7) cm, a frictional ratio of 1.2, and a sedimentation coefficient of 4.1S.

Entities: Species

Mesh：

Substances：
Sulfatases
Arylsulfatases

Year: 1981 PMID： 7204346 PMCID： PMC217151 DOI： 10.1128/jb.145.3.1428-1431.1981

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

16 in total

1. Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae.

Authors: G R Burns; C H Wynn
Journal: Biochem J Date: 1975-09 Impact factor: 3.857

2. SULFUR METABOLISM OF AEROBACTER AEROGENES. I. A REPRESSIBLE SULFATASE.

Authors: D H RAMMLER; C GRADO; L R FOWLER
Journal: Biochemistry Date: 1964-02 Impact factor: 3.162

3. A method for determining the sedimentation behavior of enzymes: application to protein mixtures.

Authors: R G MARTIN; B N AMES
Journal: J Biol Chem Date: 1961-05 Impact factor: 5.157

4. Formation and Purification of Serratia marcescens Arylsulfatase.

Authors: Y Murooka; M H Yim; T Harada
Journal: Appl Environ Microbiol Date: 1980-04 Impact factor: 4.792

5. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels.

Authors: A L Shapiro; E Viñuela; J V Maizel
Journal: Biochem Biophys Res Commun Date: 1967-09-07 Impact factor: 3.575

6. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases.

Authors: L M Siegel; K J Monty
Journal: Biochim Biophys Acta Date: 1966-02-07

Review 7. Sulfate ester formation and hydrolysis: a potentially important yet often ignored aspect of the sulfur cycle of aerobic soils.

Authors: J W Fitzgerald
Journal: Bacteriol Rev Date: 1976-09

2. Primary alkylsulphatase activities of the detergent-degrading bacterium Pseudomonas C12B. Purification and properties of the P1 enzyme.

Authors: T J Bateman; K S Dodgson; G F White
Journal: Biochem J Date: 1986-06-01 Impact factor: 3.857

2 in total

Arylsulfatase from Pseudomonas sp. strain C12B: purification to homogeneity, immunological analysis, and physical properties.

1. Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae.

2. SULFUR METABOLISM OF AEROBACTER AEROGENES. I. A REPRESSIBLE SULFATASE.

3. A method for determining the sedimentation behavior of enzymes: application to protein mixtures.

4. Formation and Purification of Serratia marcescens Arylsulfatase.

5. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels.

6. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases.

Review 7. Sulfate ester formation and hydrolysis: a potentially important yet often ignored aspect of the sulfur cycle of aerobic soils.

8. Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis.

9. Regulation of arylsulfatase synthesis by sulfur compounds in Klebsiella aerogenes.

10. Methods for visualization of enzymes in polyacrylamide gels.

1. Stimulation of bacterial arylsulfatase activity by arylamines: evidence for substrate activation.

2. Primary alkylsulphatase activities of the detergent-degrading bacterium Pseudomonas C12B. Purification and properties of the P1 enzyme.