Microanalysis of glycosaminoglycans

Moira Breen; Paul A. Knepper; Hyman G. Weinstein; Lawrence J. Blacik; Dianne G. Lewandowski; Bebe M. Baltrus

doi:10.1016/0003-2697(81)90096-8

Microanalysis of glycosaminoglycans

Moira Breen^*, Paul A. Knepper, Hyman G. Weinstein, Lawrence J. Blacik, Dianne G. Lewandowski, Bebe M. Baltrus

^*Corresponding author for this work

Ophthalmology

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22 Scopus citations

Abstract

A sensitive and versatile method for the qualitative and quantitative determination of glycosaminoglycans (GAGs) is described. An enriched GAG fraction was subjected to nuclease enzyme treatment and to an appropriate sequence of GAG degrading enzymes-Streptomyces hyaluronidase, chondroitinase AC and ABC, and endo-β-d-galactosidase-and nitrous acid treatment. To determine the result of each degradative procedure, the remaining GAG polymers were subjected to cellulose acetate electrophoresis. The combination of sequential degradation and the monitoring of each step by electrophoresis and densitometry permitted the identification and quantitation of all the GAGs on a microscale basis.

Original language	English (US)
Pages (from-to)	416-422
Number of pages	7
Journal	Analytical Biochemistry
Volume	113
Issue number	2
DOIs	https://doi.org/10.1016/0003-2697(81)90096-8
State	Published - May 15 1981

Funding

The authors gratefully acknowledge the gifts of glycosaminoglycan reference standards from Dr. Martin B. Mathews, University of Chicago, prepared under grant from National Institutes of Health, and endo+ D-galactosidase from Dr. S. Suzuki, Nagoya University. The authors wish to thank Dr. M. Litteria for helpful discussion and Ms. R. Heinz for editorial support. The authors thank Mr. Patrick Clyne for technical assistance with the cellulose acetate electrophoresis.

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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title = "Microanalysis of glycosaminoglycans",

abstract = "A sensitive and versatile method for the qualitative and quantitative determination of glycosaminoglycans (GAGs) is described. An enriched GAG fraction was subjected to nuclease enzyme treatment and to an appropriate sequence of GAG degrading enzymes-Streptomyces hyaluronidase, chondroitinase AC and ABC, and endo-β-d-galactosidase-and nitrous acid treatment. To determine the result of each degradative procedure, the remaining GAG polymers were subjected to cellulose acetate electrophoresis. The combination of sequential degradation and the monitoring of each step by electrophoresis and densitometry permitted the identification and quantitation of all the GAGs on a microscale basis.",

author = "Moira Breen and Knepper, {Paul A.} and Weinstein, {Hyman G.} and Blacik, {Lawrence J.} and Lewandowski, {Dianne G.} and Baltrus, {Bebe M.}",

note = "Funding Information: The authors gratefully acknowledge the gifts of glycosaminoglycan reference standards from Dr. Martin B. Mathews, University of Chicago, prepared under grant from National Institutes of Health, and endo+ D-galactosidase from Dr. S. Suzuki, Nagoya University. The authors wish to thank Dr. M. Litteria for helpful discussion and Ms. R. Heinz for editorial support. The authors thank Mr. Patrick Clyne for technical assistance with the cellulose acetate electrophoresis.",

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doi = "10.1016/0003-2697(81)90096-8",

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T1 - Microanalysis of glycosaminoglycans

AU - Breen, Moira

AU - Knepper, Paul A.

AU - Weinstein, Hyman G.

AU - Blacik, Lawrence J.

AU - Lewandowski, Dianne G.

AU - Baltrus, Bebe M.

N1 - Funding Information: The authors gratefully acknowledge the gifts of glycosaminoglycan reference standards from Dr. Martin B. Mathews, University of Chicago, prepared under grant from National Institutes of Health, and endo+ D-galactosidase from Dr. S. Suzuki, Nagoya University. The authors wish to thank Dr. M. Litteria for helpful discussion and Ms. R. Heinz for editorial support. The authors thank Mr. Patrick Clyne for technical assistance with the cellulose acetate electrophoresis.

PY - 1981/5/15

Y1 - 1981/5/15

N2 - A sensitive and versatile method for the qualitative and quantitative determination of glycosaminoglycans (GAGs) is described. An enriched GAG fraction was subjected to nuclease enzyme treatment and to an appropriate sequence of GAG degrading enzymes-Streptomyces hyaluronidase, chondroitinase AC and ABC, and endo-β-d-galactosidase-and nitrous acid treatment. To determine the result of each degradative procedure, the remaining GAG polymers were subjected to cellulose acetate electrophoresis. The combination of sequential degradation and the monitoring of each step by electrophoresis and densitometry permitted the identification and quantitation of all the GAGs on a microscale basis.

AB - A sensitive and versatile method for the qualitative and quantitative determination of glycosaminoglycans (GAGs) is described. An enriched GAG fraction was subjected to nuclease enzyme treatment and to an appropriate sequence of GAG degrading enzymes-Streptomyces hyaluronidase, chondroitinase AC and ABC, and endo-β-d-galactosidase-and nitrous acid treatment. To determine the result of each degradative procedure, the remaining GAG polymers were subjected to cellulose acetate electrophoresis. The combination of sequential degradation and the monitoring of each step by electrophoresis and densitometry permitted the identification and quantitation of all the GAGs on a microscale basis.

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Microanalysis of glycosaminoglycans

Abstract

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ASJC Scopus subject areas

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