Arylamidases of Crithidia fasciculata

F. B.St C. Palmer

doi:10.1016/0305-0491(74)90082-0

Arylamidases of Crithidia fasciculata

F. B.St C. Palmer

Medicine

Medicine

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

6 Citations (Scopus)

Abstract

1. 1. Crithidia fasciulata was found to be arich source of soluble enzymes hydrolysing the β-naphthylamides of leucine, arginine, lysine and glutamic acid. The specific activities were similar to values observed in mammalian tissues except for higher arylamidase A (α-glu) activity. 2. 2. Arylamidase A (α-glu) was stimulated twofold by Co²⁺, Arylamidase N (leu) was stimulated both by Co²⁺ (sixfold) and Mg²⁺ (twofold). 3. 3. The ratio of arylamidase B (arg)/arylamidase B (lys) declined from 4·2 to 1 as the cells approached the stationary growth phase.

Original language	English
Pages (from-to)	515-519
Number of pages	5
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	47
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(74)90082-0
Publication status	Published - Feb 15 1974

Bibliographical note

Funding Information:
Acknowledgements--The technical assistance of Miss L. Saulnier and Mr. A. Patrick is gratefully acknowledged. This work was supported by grants from the Medical Research Council of Canada.

ASJC Scopus Subject Areas

Biochemistry
Physiology
Molecular Biology

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10.1016/0305-0491(74)90082-0

Cite this

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title = "Arylamidases of Crithidia fasciculata",

abstract = "1. 1. Crithidia fasciulata was found to be arich source of soluble enzymes hydrolysing the β-naphthylamides of leucine, arginine, lysine and glutamic acid. The specific activities were similar to values observed in mammalian tissues except for higher arylamidase A (α-glu) activity. 2. 2. Arylamidase A (α-glu) was stimulated twofold by Co2+, Arylamidase N (leu) was stimulated both by Co2+ (sixfold) and Mg2+ (twofold). 3. 3. The ratio of arylamidase B (arg)/arylamidase B (lys) declined from 4·2 to 1 as the cells approached the stationary growth phase.",

author = "Palmer, {F. B.St C.}",

note = "Funding Information: Acknowledgements--The technical assistance of Miss L. Saulnier and Mr. A. Patrick is gratefully acknowledged. This work was supported by grants from the Medical Research Council of Canada.",

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T1 - Arylamidases of Crithidia fasciculata

AU - Palmer, F. B.St C.

N1 - Funding Information: Acknowledgements--The technical assistance of Miss L. Saulnier and Mr. A. Patrick is gratefully acknowledged. This work was supported by grants from the Medical Research Council of Canada.

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N2 - 1. 1. Crithidia fasciulata was found to be arich source of soluble enzymes hydrolysing the β-naphthylamides of leucine, arginine, lysine and glutamic acid. The specific activities were similar to values observed in mammalian tissues except for higher arylamidase A (α-glu) activity. 2. 2. Arylamidase A (α-glu) was stimulated twofold by Co2+, Arylamidase N (leu) was stimulated both by Co2+ (sixfold) and Mg2+ (twofold). 3. 3. The ratio of arylamidase B (arg)/arylamidase B (lys) declined from 4·2 to 1 as the cells approached the stationary growth phase.

AB - 1. 1. Crithidia fasciulata was found to be arich source of soluble enzymes hydrolysing the β-naphthylamides of leucine, arginine, lysine and glutamic acid. The specific activities were similar to values observed in mammalian tissues except for higher arylamidase A (α-glu) activity. 2. 2. Arylamidase A (α-glu) was stimulated twofold by Co2+, Arylamidase N (leu) was stimulated both by Co2+ (sixfold) and Mg2+ (twofold). 3. 3. The ratio of arylamidase B (arg)/arylamidase B (lys) declined from 4·2 to 1 as the cells approached the stationary growth phase.

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JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

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Arylamidases of Crithidia fasciculata

Abstract

Bibliographical note

ASJC Scopus Subject Areas

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