Characteristics and distribution of extracellular proteases from Aeromonas hydrophila

K. Y. Leung; R. M.W. Stevenson

doi:10.1099/00221287-134-1-151

Characteristics and distribution of extracellular proteases from Aeromonas hydrophila

K. Y. Leung, R. M.W. Stevenson

Research output: Contribution to journal › Article › peer-review

82 Scopus citations

Abstract

The major extracellular proteases of Aeromonas hydrophila NRC 505 and ATCC 7966 are a thermostable metallo-protease (TSMP) and a thermolabile serine-protease (TLSP), respectively. The purified enzymes differed in sensitivity to heating at 56°C for 30 min, in response to the inhibitors EDTA and phenylmethylsulphonyl fluoride (PMSF), and were antigenically distinct. When crude extracellular products (ECP) of 47 strains of A. hydrophila were screened, 27 strains produced both TSMP and TLSP. TSMP was the only extracellular protease produced by 19 strains, whereas only A. hydrophila ATCC 7966 produced TLSP as its sole protease. This distribution of protease enzymes among strains explains conflicting reports from studies in which single strains of A. hydrophila were examined. The TLSP of A. hydrophila was similar to the protease of A. salmonicida. Either or both TSMP and TLSP were produced by some strains of A. sobria and A. caviae.

Original language	English
Pages (from-to)	151-160
Number of pages	10
Journal	Journal of General Microbiology
Volume	134
Issue number	1
DOIs	https://doi.org/10.1099/00221287-134-1-151
State	Published - 1988
Externally published	Yes

Access to Document

10.1099/00221287-134-1-151

Cite this

@article{aba6c33518234c9898fb3e68c097c870,

title = "Characteristics and distribution of extracellular proteases from Aeromonas hydrophila",

abstract = "The major extracellular proteases of Aeromonas hydrophila NRC 505 and ATCC 7966 are a thermostable metallo-protease (TSMP) and a thermolabile serine-protease (TLSP), respectively. The purified enzymes differed in sensitivity to heating at 56°C for 30 min, in response to the inhibitors EDTA and phenylmethylsulphonyl fluoride (PMSF), and were antigenically distinct. When crude extracellular products (ECP) of 47 strains of A. hydrophila were screened, 27 strains produced both TSMP and TLSP. TSMP was the only extracellular protease produced by 19 strains, whereas only A. hydrophila ATCC 7966 produced TLSP as its sole protease. This distribution of protease enzymes among strains explains conflicting reports from studies in which single strains of A. hydrophila were examined. The TLSP of A. hydrophila was similar to the protease of A. salmonicida. Either or both TSMP and TLSP were produced by some strains of A. sobria and A. caviae.",

author = "Leung, {K. Y.} and Stevenson, {R. M.W.}",

year = "1988",

doi = "10.1099/00221287-134-1-151",

language = "英语",

volume = "134",

pages = "151--160",

journal = "Journal of General Microbiology",

issn = "0022-1287",

publisher = "Microbiology Society",

number = "1",

}

TY - JOUR

T1 - Characteristics and distribution of extracellular proteases from Aeromonas hydrophila

AU - Leung, K. Y.

AU - Stevenson, R. M.W.

PY - 1988

Y1 - 1988

N2 - The major extracellular proteases of Aeromonas hydrophila NRC 505 and ATCC 7966 are a thermostable metallo-protease (TSMP) and a thermolabile serine-protease (TLSP), respectively. The purified enzymes differed in sensitivity to heating at 56°C for 30 min, in response to the inhibitors EDTA and phenylmethylsulphonyl fluoride (PMSF), and were antigenically distinct. When crude extracellular products (ECP) of 47 strains of A. hydrophila were screened, 27 strains produced both TSMP and TLSP. TSMP was the only extracellular protease produced by 19 strains, whereas only A. hydrophila ATCC 7966 produced TLSP as its sole protease. This distribution of protease enzymes among strains explains conflicting reports from studies in which single strains of A. hydrophila were examined. The TLSP of A. hydrophila was similar to the protease of A. salmonicida. Either or both TSMP and TLSP were produced by some strains of A. sobria and A. caviae.

AB - The major extracellular proteases of Aeromonas hydrophila NRC 505 and ATCC 7966 are a thermostable metallo-protease (TSMP) and a thermolabile serine-protease (TLSP), respectively. The purified enzymes differed in sensitivity to heating at 56°C for 30 min, in response to the inhibitors EDTA and phenylmethylsulphonyl fluoride (PMSF), and were antigenically distinct. When crude extracellular products (ECP) of 47 strains of A. hydrophila were screened, 27 strains produced both TSMP and TLSP. TSMP was the only extracellular protease produced by 19 strains, whereas only A. hydrophila ATCC 7966 produced TLSP as its sole protease. This distribution of protease enzymes among strains explains conflicting reports from studies in which single strains of A. hydrophila were examined. The TLSP of A. hydrophila was similar to the protease of A. salmonicida. Either or both TSMP and TLSP were produced by some strains of A. sobria and A. caviae.

UR - http://www.scopus.com/inward/record.url?scp=0023883140&partnerID=8YFLogxK

U2 - 10.1099/00221287-134-1-151

DO - 10.1099/00221287-134-1-151

M3 - 文章

AN - SCOPUS:0023883140

SN - 0022-1287

VL - 134

SP - 151

EP - 160

JO - Journal of General Microbiology

JF - Journal of General Microbiology

IS - 1

ER -

Characteristics and distribution of extracellular proteases from Aeromonas hydrophila

Abstract

Access to Document

Other files and links

Fingerprint

Cite this