Isolation and characterization of pig muscle aldolase. a comparative study

Magdolna Ábrahám, Lóránt Horváth, B. Szajáni

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

1. 1. Aldolase with a specific activity of 10.8 units/mg protein was isolated from pig muscle. 2. 2. Its molecular weight was found to be 150,000. The optimum pH for the catalytic activity was 7.25 and the apparent temperature optimum was 313 K. The Km value was 2.9 × 10-5M with FDP as substrate, and 2.8 × 10-3M with F1P as substrate. 3. 3. The thermal stability of this pig muscle enzyme was higher than that of the rabbit muscle enzyme. The thermal inactivation of the pig aldolase did not show simple first-order kinetics. 4. 4. The higher conformational stability of the pig aldolase than that of the rabbit enzyme was demonstrated by its higher resistance to the denaturing effect of urea.

Original languageEnglish
Pages (from-to)847-852
Number of pages6
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume80
Issue number4
DOIs
Publication statusPublished - 1985

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Fructose-Bisphosphate Aldolase
Muscle
Swine
Muscles
Enzymes
Hot Temperature
Substrates
Rabbits
Urea
Catalyst activity
Thermodynamic stability
Molecular weight
Kinetics
Molecular Weight
Temperature
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Isolation and characterization of pig muscle aldolase. a comparative study. / Ábrahám, Magdolna; Horváth, Lóránt; Szajáni, B.

In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 80, No. 4, 1985, p. 847-852.

Research output: Contribution to journalArticle

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