Microdetermination of aldose and aldehyde reductases from human tissues

Hui Ping Song, Ballabh Das, Satish Srivastava

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Microfluofometric method has been described for the determination of aldose reductase and aldehyde reductase II activities in human erythrocyte, brain, and lens. The enzyme activity determined by the microfluorometric method was compared with the activity determined spectrophotometrically by following the oxidation of NADPH and fluorometrically by the formation of sorbitol. The activity of aldose reductase in homogenous preparations from human lens, brain, and erythrocyte was identical when determined by NADPH oxidation, NADP formation, and sorbitol formation using glucose as substrate and NADPH as co-factor. This indicated that NADPH oxidation by aldose reductase is not due to a non-specific oxidation by oxidants generated as a result of interaction of aldose reductase and glucose. Similarly, the activity of aldehyde reductase II obtained by NADPH oxidation and that by NADP formation were in good agreement. The microfluorescent method is convenient and accurate and can be used for the. determination of aldose reductase in human tissues using glucose as substrate even when the sample size is small.

Original languageEnglish (US)
Pages (from-to)1001-1006
Number of pages6
JournalCurrent Eye Research
Volume6
Issue number8
DOIs
StatePublished - 1987

Fingerprint

Aldehyde Reductase
NADP
L-glucuronate reductase
Sorbitol
Glucose
Lenses
Erythrocytes
Brain
Oxidants
Human Activities
Sample Size
Enzymes

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Cite this

Microdetermination of aldose and aldehyde reductases from human tissues. / Song, Hui Ping; Das, Ballabh; Srivastava, Satish.

In: Current Eye Research, Vol. 6, No. 8, 1987, p. 1001-1006.

Research output: Contribution to journalArticle

Song, Hui Ping ; Das, Ballabh ; Srivastava, Satish. / Microdetermination of aldose and aldehyde reductases from human tissues. In: Current Eye Research. 1987 ; Vol. 6, No. 8. pp. 1001-1006.
@article{fa110bc46a274aecbb06dd33e8ae3f9a,
title = "Microdetermination of aldose and aldehyde reductases from human tissues",
abstract = "Microfluofometric method has been described for the determination of aldose reductase and aldehyde reductase II activities in human erythrocyte, brain, and lens. The enzyme activity determined by the microfluorometric method was compared with the activity determined spectrophotometrically by following the oxidation of NADPH and fluorometrically by the formation of sorbitol. The activity of aldose reductase in homogenous preparations from human lens, brain, and erythrocyte was identical when determined by NADPH oxidation, NADP formation, and sorbitol formation using glucose as substrate and NADPH as co-factor. This indicated that NADPH oxidation by aldose reductase is not due to a non-specific oxidation by oxidants generated as a result of interaction of aldose reductase and glucose. Similarly, the activity of aldehyde reductase II obtained by NADPH oxidation and that by NADP formation were in good agreement. The microfluorescent method is convenient and accurate and can be used for the. determination of aldose reductase in human tissues using glucose as substrate even when the sample size is small.",
author = "Song, {Hui Ping} and Ballabh Das and Satish Srivastava",
year = "1987",
doi = "10.3109/02713688709034871",
language = "English (US)",
volume = "6",
pages = "1001--1006",
journal = "Current Eye Research",
issn = "0271-3683",
publisher = "Informa Healthcare",
number = "8",

}

TY - JOUR

T1 - Microdetermination of aldose and aldehyde reductases from human tissues

AU - Song, Hui Ping

AU - Das, Ballabh

AU - Srivastava, Satish

PY - 1987

Y1 - 1987

N2 - Microfluofometric method has been described for the determination of aldose reductase and aldehyde reductase II activities in human erythrocyte, brain, and lens. The enzyme activity determined by the microfluorometric method was compared with the activity determined spectrophotometrically by following the oxidation of NADPH and fluorometrically by the formation of sorbitol. The activity of aldose reductase in homogenous preparations from human lens, brain, and erythrocyte was identical when determined by NADPH oxidation, NADP formation, and sorbitol formation using glucose as substrate and NADPH as co-factor. This indicated that NADPH oxidation by aldose reductase is not due to a non-specific oxidation by oxidants generated as a result of interaction of aldose reductase and glucose. Similarly, the activity of aldehyde reductase II obtained by NADPH oxidation and that by NADP formation were in good agreement. The microfluorescent method is convenient and accurate and can be used for the. determination of aldose reductase in human tissues using glucose as substrate even when the sample size is small.

AB - Microfluofometric method has been described for the determination of aldose reductase and aldehyde reductase II activities in human erythrocyte, brain, and lens. The enzyme activity determined by the microfluorometric method was compared with the activity determined spectrophotometrically by following the oxidation of NADPH and fluorometrically by the formation of sorbitol. The activity of aldose reductase in homogenous preparations from human lens, brain, and erythrocyte was identical when determined by NADPH oxidation, NADP formation, and sorbitol formation using glucose as substrate and NADPH as co-factor. This indicated that NADPH oxidation by aldose reductase is not due to a non-specific oxidation by oxidants generated as a result of interaction of aldose reductase and glucose. Similarly, the activity of aldehyde reductase II obtained by NADPH oxidation and that by NADP formation were in good agreement. The microfluorescent method is convenient and accurate and can be used for the. determination of aldose reductase in human tissues using glucose as substrate even when the sample size is small.

UR - http://www.scopus.com/inward/record.url?scp=0023222441&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023222441&partnerID=8YFLogxK

U2 - 10.3109/02713688709034871

DO - 10.3109/02713688709034871

M3 - Article

C2 - 3117493

AN - SCOPUS:0023222441

VL - 6

SP - 1001

EP - 1006

JO - Current Eye Research

JF - Current Eye Research

SN - 0271-3683

IS - 8

ER -