Enzyme therapy-IX. stabilization of human splenic α-galactosidase a by zinc ion

Suzanne R. Thorpe; Robert J. Desnick

doi:10.1016/0020-711X(78)90019-8

Enzyme therapy-IX. stabilization of human splenic α-galactosidase a by zinc ion

Suzanne R. Thorpe
, Robert J. Desnick

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

Abstract

1. 1. The ability of divalent metal ions to stabilize several human lysosomal glycosidases against thermal inactivation was investigated. 2. 2. Only zinc ion was found to significantly decrease the rate of heat denaturation of any of the hydrolases tested. 3. 3. Zinc increased the t_{1 2} of a-galactosidase A activity at 50°C more than 15-fold at pH 6.5, from 20.5 min to 5.2 hr, but had little effect at pH 5.5 or 7.4.

Original language	English
Pages (from-to)	103-105
Number of pages	3
Journal	International Journal of Biochemistry
Volume	9
Issue number	2
DOIs	https://doi.org/10.1016/0020-711X(78)90019-8
State	Published - 1978
Externally published	Yes

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@article{1eb7aac7b0b048a38a40bfb0a682e8cb,

title = "Enzyme therapy-IX. stabilization of human splenic α-galactosidase a by zinc ion",

abstract = "1. 1. The ability of divalent metal ions to stabilize several human lysosomal glycosidases against thermal inactivation was investigated. 2. 2. Only zinc ion was found to significantly decrease the rate of heat denaturation of any of the hydrolases tested. 3. 3. Zinc increased the t 1 2 of a-galactosidase A activity at 50°C more than 15-fold at pH 6.5, from 20.5 min to 5.2 hr, but had little effect at pH 5.5 or 7.4.",

author = "Thorpe, \{Suzanne R.\} and Desnick, \{Robert J.\}",

note = "Funding Information: Ac\textasciitilde{}noulet/gemc,rltsThe authors wish to express their grateful appreciation to MS Carolyn Dullum for her technical assistance and to MS Ardys Moen for her expert clerical assistance. This work was supported in part by grants from the National Foundation-March of Dimes (l-273). and the National Institutes of Health (AM 15174). S. R. Thorpe was a recipient of a National Institutes of Health postdoctoral training fellowship (IT22 00025) and R. J. Desnick is the recipient of a National Institute of Health Research Career Development Award (AM 00042).",

year = "1978",

doi = "10.1016/0020-711X(78)90019-8",

language = "English",

volume = "9",

pages = "103--105",

journal = "International Journal of Biochemistry",

issn = "0020-711X",

publisher = "Elsevier Ltd.",

number = "2",

}

TY - JOUR

T1 - Enzyme therapy-IX. stabilization of human splenic α-galactosidase a by zinc ion

AU - Thorpe, Suzanne R.

AU - Desnick, Robert J.

N1 - Funding Information: Ac~noulet/gemc,rltsThe authors wish to express their grateful appreciation to MS Carolyn Dullum for her technical assistance and to MS Ardys Moen for her expert clerical assistance. This work was supported in part by grants from the National Foundation-March of Dimes (l-273). and the National Institutes of Health (AM 15174). S. R. Thorpe was a recipient of a National Institutes of Health postdoctoral training fellowship (IT22 00025) and R. J. Desnick is the recipient of a National Institute of Health Research Career Development Award (AM 00042).

PY - 1978

Y1 - 1978

N2 - 1. 1. The ability of divalent metal ions to stabilize several human lysosomal glycosidases against thermal inactivation was investigated. 2. 2. Only zinc ion was found to significantly decrease the rate of heat denaturation of any of the hydrolases tested. 3. 3. Zinc increased the t 1 2 of a-galactosidase A activity at 50°C more than 15-fold at pH 6.5, from 20.5 min to 5.2 hr, but had little effect at pH 5.5 or 7.4.

AB - 1. 1. The ability of divalent metal ions to stabilize several human lysosomal glycosidases against thermal inactivation was investigated. 2. 2. Only zinc ion was found to significantly decrease the rate of heat denaturation of any of the hydrolases tested. 3. 3. Zinc increased the t 1 2 of a-galactosidase A activity at 50°C more than 15-fold at pH 6.5, from 20.5 min to 5.2 hr, but had little effect at pH 5.5 or 7.4.

UR - https://www.scopus.com/pages/publications/0017883749

U2 - 10.1016/0020-711X(78)90019-8

DO - 10.1016/0020-711X(78)90019-8

M3 - Article

C2 - 205451

AN - SCOPUS:0017883749

SN - 0020-711X

VL - 9

SP - 103

EP - 105

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

IS - 2

ER -

Enzyme therapy-IX. stabilization of human splenic α-galactosidase a by zinc ion

Abstract

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