Angiontensin-converting enzyme activity in dunning rat prostate tumor

M. J. Wilson; M. S. Mack; M. Woodson; A. A. Sinha

doi:10.1080/01485010390236314

Angiontensin-converting enzyme activity in dunning rat prostate tumor

M. J. Wilson, M. S. Mack, M. Woodson, A. A. Sinha

Urology

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

1 Scopus citations

Abstract

A dipeptidyl carboxypeptidase activity in the Dunning rat prostate tumor was characterized. This enzyme demonstrated the most prominent properties of angiotensin converting enzyme (ACE): that is, it was stimulated by NaCl and Co²⁺ and was potently inhibited by captopril. The enzyme solubilized by Triton X-100 had a molecular mass of 110 kDa as determined by gel filtration chromatography. The specific activity of ACE did not change with castration, indicating that ACE activities are not controlled by androgen. The role of ACE in the prostate and its tumors is not understood, but the ability of this enzyme to hydrolyze a number of bioactive peptides suggests that it may function in controlling the molecular forms or activity of regulatory peptides.

Original language	English (US)
Pages (from-to)	457-461
Number of pages	5
Journal	Archives of Andrology
Volume	49
Issue number	6
DOIs	https://doi.org/10.1080/01485010390236314
State	Published - Jan 1 2003

Keywords

ACE
Angiotensin-converting enzyme
Peptidase
Prostate
Rat

Publisher link

10.1080/01485010390236314

Find It

Find It at U of M Libraries

Cite this

@article{0d4ec83bfff64f8ebe59793c1e3657f2,

title = "Angiontensin-converting enzyme activity in dunning rat prostate tumor",

abstract = "A dipeptidyl carboxypeptidase activity in the Dunning rat prostate tumor was characterized. This enzyme demonstrated the most prominent properties of angiotensin converting enzyme (ACE): that is, it was stimulated by NaCl and Co2+ and was potently inhibited by captopril. The enzyme solubilized by Triton X-100 had a molecular mass of 110 kDa as determined by gel filtration chromatography. The specific activity of ACE did not change with castration, indicating that ACE activities are not controlled by androgen. The role of ACE in the prostate and its tumors is not understood, but the ability of this enzyme to hydrolyze a number of bioactive peptides suggests that it may function in controlling the molecular forms or activity of regulatory peptides.",

keywords = "ACE, Angiotensin-converting enzyme, Peptidase, Prostate, Rat",

author = "Wilson, {M. J.} and Mack, {M. S.} and M. Woodson and Sinha, {A. A.}",

year = "2003",

month = jan,

day = "1",

doi = "10.1080/01485010390236314",

language = "English (US)",

volume = "49",

pages = "457--461",

journal = "Systems Biology in Reproductive Medicine",

issn = "1939-6368",

publisher = "Informa Healthcare",

number = "6",

}

TY - JOUR

T1 - Angiontensin-converting enzyme activity in dunning rat prostate tumor

AU - Wilson, M. J.

AU - Mack, M. S.

AU - Woodson, M.

AU - Sinha, A. A.

PY - 2003/1/1

Y1 - 2003/1/1

N2 - A dipeptidyl carboxypeptidase activity in the Dunning rat prostate tumor was characterized. This enzyme demonstrated the most prominent properties of angiotensin converting enzyme (ACE): that is, it was stimulated by NaCl and Co2+ and was potently inhibited by captopril. The enzyme solubilized by Triton X-100 had a molecular mass of 110 kDa as determined by gel filtration chromatography. The specific activity of ACE did not change with castration, indicating that ACE activities are not controlled by androgen. The role of ACE in the prostate and its tumors is not understood, but the ability of this enzyme to hydrolyze a number of bioactive peptides suggests that it may function in controlling the molecular forms or activity of regulatory peptides.

AB - A dipeptidyl carboxypeptidase activity in the Dunning rat prostate tumor was characterized. This enzyme demonstrated the most prominent properties of angiotensin converting enzyme (ACE): that is, it was stimulated by NaCl and Co2+ and was potently inhibited by captopril. The enzyme solubilized by Triton X-100 had a molecular mass of 110 kDa as determined by gel filtration chromatography. The specific activity of ACE did not change with castration, indicating that ACE activities are not controlled by androgen. The role of ACE in the prostate and its tumors is not understood, but the ability of this enzyme to hydrolyze a number of bioactive peptides suggests that it may function in controlling the molecular forms or activity of regulatory peptides.

KW - ACE

KW - Angiotensin-converting enzyme

KW - Peptidase

KW - Prostate

KW - Rat

UR - http://www.scopus.com/inward/record.url?scp=79961177647&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79961177647&partnerID=8YFLogxK

U2 - 10.1080/01485010390236314

DO - 10.1080/01485010390236314

M3 - Article

AN - SCOPUS:79961177647

SN - 1939-6368

VL - 49

SP - 457

EP - 461

JO - Systems Biology in Reproductive Medicine

JF - Systems Biology in Reproductive Medicine

IS - 6

ER -

Angiontensin-converting enzyme activity in dunning rat prostate tumor

Abstract

Keywords

Publisher link

Find It

Other files and links

Fingerprint

Cite this