Electrophoretic separation of neutral and acid β-glucosidase isozymes in human tissues

Bridget Shafit-Zagardo, E. A. Devine, R. J. Desnick

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

An electrophoretic system using cellulose acetate has been developed for the resolution of β-glucosidase isozymes (β-D-glucoside glucohydrolase, EC 3.2.1.21 and D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) in human tissue homogenates. Electrophoresis of homogenates from normal and Type I Gaucher disease tissues revealed two fluorescent bands of β-glucosidase activity which corresponded to the acid and neutral isozymes separated by concanavalin A-Sepharose chromatography. The acid isozyme had only β-glucosidase activity, whereas the neutral isozyme also exhibited α-L-arabinosidase (α-L-arabino-furanoside arabinofuranohydrolase, EC 3.2.1.55), β-D-galactosidase (β-D galactoside galactohydrolase, , EC 3.2.1.23) and β-D-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) activities, using the appropriate 4-methylumbelliferyl glycoside. In homogenates of cultured skin fibroblasts, only the acid isozyme was observed which co-electrophoresed with the acidic activity in other tissue homogenates. The acidic activity in tissue and fibroblast homogenates from Type I Gaucher disease appeared to co-electrophorese with the acid isozyme in normal tissues, but had markedly reduced activity.

Original languageEnglish (US)
Pages (from-to)459-465
Number of pages7
JournalBiochimica et Biophysica Acta
Volume614
Issue number2
StatePublished - 1980
Externally publishedYes

Fingerprint

Glucosidases
Isoenzymes
Tissue
Acids
Gaucher Disease
Fibroblasts
Xylosidases
Xylans
Galactosides
Agarose Chromatography
Glucosides
Chromatography
Electrophoresis
Skin

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Electrophoretic separation of neutral and acid β-glucosidase isozymes in human tissues. / Shafit-Zagardo, Bridget; Devine, E. A.; Desnick, R. J.

In: Biochimica et Biophysica Acta, Vol. 614, No. 2, 1980, p. 459-465.

Research output: Contribution to journalArticle

@article{d0b6628b1ec94d3f96af6f544e806c88,
title = "Electrophoretic separation of neutral and acid β-glucosidase isozymes in human tissues",
abstract = "An electrophoretic system using cellulose acetate has been developed for the resolution of β-glucosidase isozymes (β-D-glucoside glucohydrolase, EC 3.2.1.21 and D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) in human tissue homogenates. Electrophoresis of homogenates from normal and Type I Gaucher disease tissues revealed two fluorescent bands of β-glucosidase activity which corresponded to the acid and neutral isozymes separated by concanavalin A-Sepharose chromatography. The acid isozyme had only β-glucosidase activity, whereas the neutral isozyme also exhibited α-L-arabinosidase (α-L-arabino-furanoside arabinofuranohydrolase, EC 3.2.1.55), β-D-galactosidase (β-D galactoside galactohydrolase, , EC 3.2.1.23) and β-D-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) activities, using the appropriate 4-methylumbelliferyl glycoside. In homogenates of cultured skin fibroblasts, only the acid isozyme was observed which co-electrophoresed with the acidic activity in other tissue homogenates. The acidic activity in tissue and fibroblast homogenates from Type I Gaucher disease appeared to co-electrophorese with the acid isozyme in normal tissues, but had markedly reduced activity.",
author = "Bridget Shafit-Zagardo and Devine, {E. A.} and Desnick, {R. J.}",
year = "1980",
language = "English (US)",
volume = "614",
pages = "459--465",
journal = "Biochimica et Biophysica Acta - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Electrophoretic separation of neutral and acid β-glucosidase isozymes in human tissues

AU - Shafit-Zagardo, Bridget

AU - Devine, E. A.

AU - Desnick, R. J.

PY - 1980

Y1 - 1980

N2 - An electrophoretic system using cellulose acetate has been developed for the resolution of β-glucosidase isozymes (β-D-glucoside glucohydrolase, EC 3.2.1.21 and D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) in human tissue homogenates. Electrophoresis of homogenates from normal and Type I Gaucher disease tissues revealed two fluorescent bands of β-glucosidase activity which corresponded to the acid and neutral isozymes separated by concanavalin A-Sepharose chromatography. The acid isozyme had only β-glucosidase activity, whereas the neutral isozyme also exhibited α-L-arabinosidase (α-L-arabino-furanoside arabinofuranohydrolase, EC 3.2.1.55), β-D-galactosidase (β-D galactoside galactohydrolase, , EC 3.2.1.23) and β-D-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) activities, using the appropriate 4-methylumbelliferyl glycoside. In homogenates of cultured skin fibroblasts, only the acid isozyme was observed which co-electrophoresed with the acidic activity in other tissue homogenates. The acidic activity in tissue and fibroblast homogenates from Type I Gaucher disease appeared to co-electrophorese with the acid isozyme in normal tissues, but had markedly reduced activity.

AB - An electrophoretic system using cellulose acetate has been developed for the resolution of β-glucosidase isozymes (β-D-glucoside glucohydrolase, EC 3.2.1.21 and D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) in human tissue homogenates. Electrophoresis of homogenates from normal and Type I Gaucher disease tissues revealed two fluorescent bands of β-glucosidase activity which corresponded to the acid and neutral isozymes separated by concanavalin A-Sepharose chromatography. The acid isozyme had only β-glucosidase activity, whereas the neutral isozyme also exhibited α-L-arabinosidase (α-L-arabino-furanoside arabinofuranohydrolase, EC 3.2.1.55), β-D-galactosidase (β-D galactoside galactohydrolase, , EC 3.2.1.23) and β-D-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) activities, using the appropriate 4-methylumbelliferyl glycoside. In homogenates of cultured skin fibroblasts, only the acid isozyme was observed which co-electrophoresed with the acidic activity in other tissue homogenates. The acidic activity in tissue and fibroblast homogenates from Type I Gaucher disease appeared to co-electrophorese with the acid isozyme in normal tissues, but had markedly reduced activity.

UR - http://www.scopus.com/inward/record.url?scp=0019120325&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019120325&partnerID=8YFLogxK

M3 - Article

C2 - 6773581

AN - SCOPUS:0019120325

VL - 614

SP - 459

EP - 465

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

SN - 0304-4165

IS - 2

ER -