Alkaline phosphatases from clinical and non clinical strains of Serratia marcescens grown in two types of media

David M Kranz, L. V. Page, J. C. Tsang

Research output: Contribution to journalArticle

Abstract

The release and characterization of alkaline phosphatases from a clinical and a non clinical strain of S. marcescens grown in two types of media were studied. Four different identifiable alkaline phosphatases (A', A, B, and E) were found to be releasable by polymyxin B treatment of whole cells grown in an inorganic phosphate free casamino acid medium, one of which, component B, was also releasable by saline wash from cells grown in a high inorganic phosphate glucose medium. SDS polyacrylamide gel electrophoresis followed by incubation of the gels in p nitrophenyl phosphate showed that there were three very active polymeric components (A', A, and B) with molecular weights of 190,000 ± 10,000, 140,000 ± 10,000, and 110,000 ± 10,000, respectively, and one possibly monomeric component, E, with molecular weight of 44,000 ± 1,000. Alkaline phosphatase B was present in both types of medium and was considered constitutive. However, the other two active alkaline phosphatases A', and A were present only in cells grown in the inorganic phosphate free casamino acid medium. By incubation at two temperatures (37°C and 70°C), prior to electrophoresis and enzyme assay, only component A remained active at 70°C. It is concluded that among the four alkaline phosphatases detected, one was a monomer (E), one was constitutive (B), and the remaining two (A' and A) were possibly inducible by an inorganic phosphate free medium. In addition, the effectiveness of polymyxin B on the release of periplasmic enzymes from cells of S. marcescens grown in different types of medium was discussed.

Original languageEnglish (US)
Pages (from-to)183-193
Number of pages11
JournalMicrobios
Volume14
Issue number58
StatePublished - Jan 1 1975
Externally publishedYes

Fingerprint

Serratia marcescens
Alkaline Phosphatase
Phosphates
Polymyxin B
Molecular Weight
Enzyme Assays
Electrophoresis
Polyacrylamide Gel Electrophoresis
Gels
Glucose
Temperature
Enzymes

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Cite this

Alkaline phosphatases from clinical and non clinical strains of Serratia marcescens grown in two types of media. / Kranz, David M; Page, L. V.; Tsang, J. C.

In: Microbios, Vol. 14, No. 58, 01.01.1975, p. 183-193.

Research output: Contribution to journalArticle

@article{64a30aabe2e74cd3b83ece90725c89a6,
title = "Alkaline phosphatases from clinical and non clinical strains of Serratia marcescens grown in two types of media",
abstract = "The release and characterization of alkaline phosphatases from a clinical and a non clinical strain of S. marcescens grown in two types of media were studied. Four different identifiable alkaline phosphatases (A', A, B, and E) were found to be releasable by polymyxin B treatment of whole cells grown in an inorganic phosphate free casamino acid medium, one of which, component B, was also releasable by saline wash from cells grown in a high inorganic phosphate glucose medium. SDS polyacrylamide gel electrophoresis followed by incubation of the gels in p nitrophenyl phosphate showed that there were three very active polymeric components (A', A, and B) with molecular weights of 190,000 ± 10,000, 140,000 ± 10,000, and 110,000 ± 10,000, respectively, and one possibly monomeric component, E, with molecular weight of 44,000 ± 1,000. Alkaline phosphatase B was present in both types of medium and was considered constitutive. However, the other two active alkaline phosphatases A', and A were present only in cells grown in the inorganic phosphate free casamino acid medium. By incubation at two temperatures (37°C and 70°C), prior to electrophoresis and enzyme assay, only component A remained active at 70°C. It is concluded that among the four alkaline phosphatases detected, one was a monomer (E), one was constitutive (B), and the remaining two (A' and A) were possibly inducible by an inorganic phosphate free medium. In addition, the effectiveness of polymyxin B on the release of periplasmic enzymes from cells of S. marcescens grown in different types of medium was discussed.",
author = "Kranz, {David M} and Page, {L. V.} and Tsang, {J. C.}",
year = "1975",
month = "1",
day = "1",
language = "English (US)",
volume = "14",
pages = "183--193",
journal = "Microbios",
issn = "0026-2633",
publisher = "University of Cambridge",
number = "58",

}

TY - JOUR

T1 - Alkaline phosphatases from clinical and non clinical strains of Serratia marcescens grown in two types of media

AU - Kranz, David M

AU - Page, L. V.

AU - Tsang, J. C.

PY - 1975/1/1

Y1 - 1975/1/1

N2 - The release and characterization of alkaline phosphatases from a clinical and a non clinical strain of S. marcescens grown in two types of media were studied. Four different identifiable alkaline phosphatases (A', A, B, and E) were found to be releasable by polymyxin B treatment of whole cells grown in an inorganic phosphate free casamino acid medium, one of which, component B, was also releasable by saline wash from cells grown in a high inorganic phosphate glucose medium. SDS polyacrylamide gel electrophoresis followed by incubation of the gels in p nitrophenyl phosphate showed that there were three very active polymeric components (A', A, and B) with molecular weights of 190,000 ± 10,000, 140,000 ± 10,000, and 110,000 ± 10,000, respectively, and one possibly monomeric component, E, with molecular weight of 44,000 ± 1,000. Alkaline phosphatase B was present in both types of medium and was considered constitutive. However, the other two active alkaline phosphatases A', and A were present only in cells grown in the inorganic phosphate free casamino acid medium. By incubation at two temperatures (37°C and 70°C), prior to electrophoresis and enzyme assay, only component A remained active at 70°C. It is concluded that among the four alkaline phosphatases detected, one was a monomer (E), one was constitutive (B), and the remaining two (A' and A) were possibly inducible by an inorganic phosphate free medium. In addition, the effectiveness of polymyxin B on the release of periplasmic enzymes from cells of S. marcescens grown in different types of medium was discussed.

AB - The release and characterization of alkaline phosphatases from a clinical and a non clinical strain of S. marcescens grown in two types of media were studied. Four different identifiable alkaline phosphatases (A', A, B, and E) were found to be releasable by polymyxin B treatment of whole cells grown in an inorganic phosphate free casamino acid medium, one of which, component B, was also releasable by saline wash from cells grown in a high inorganic phosphate glucose medium. SDS polyacrylamide gel electrophoresis followed by incubation of the gels in p nitrophenyl phosphate showed that there were three very active polymeric components (A', A, and B) with molecular weights of 190,000 ± 10,000, 140,000 ± 10,000, and 110,000 ± 10,000, respectively, and one possibly monomeric component, E, with molecular weight of 44,000 ± 1,000. Alkaline phosphatase B was present in both types of medium and was considered constitutive. However, the other two active alkaline phosphatases A', and A were present only in cells grown in the inorganic phosphate free casamino acid medium. By incubation at two temperatures (37°C and 70°C), prior to electrophoresis and enzyme assay, only component A remained active at 70°C. It is concluded that among the four alkaline phosphatases detected, one was a monomer (E), one was constitutive (B), and the remaining two (A' and A) were possibly inducible by an inorganic phosphate free medium. In addition, the effectiveness of polymyxin B on the release of periplasmic enzymes from cells of S. marcescens grown in different types of medium was discussed.

UR - http://www.scopus.com/inward/record.url?scp=0016584888&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016584888&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0016584888

VL - 14

SP - 183

EP - 193

JO - Microbios

JF - Microbios

SN - 0026-2633

IS - 58

ER -