Multiple Molecular Forms of Avian Aldolases. VI. Enzymatic Properties and Amino Acid Composition of Chicken Liver Aldolase and Comparative Immunochemical Properties

Author:

Marquardt Ronald R.

Abstract

Several properties of pure chicken (Gallus domesticus) liver aldolase (fructose-1,6-diphosphate D-glycer-aldehyde-3-phosphate-lyase, EC 4.1.2.13) were determined. The enzyme shows a broad pH optimum peaking around pH 7.7, is stable over a wide pH range, and has a temperature coefficient Q10 of 2.3. The enzyme is stable at 48 °C for 10 min and is almost completely inactivated at 55 °C.The amino acid composition of pure chicken liver aldolase was determined. Its composition was compared with those of chicken muscle and chicken brain aldolases and with the corresponding rabbit aldolase enzymes.Antiserum was prepared against purified chicken liver aldolase and the immunological properties of aldolases from various tissues and species were examined. In the chicken, the antiserum has a very pronounced reaction with liver and kidney aldolases but only a weak cross-reaction with either the brain or the muscle enzyme. The antiserum readily cross-reacts with other avian liver aldolases (turkey and budgerigar) but not with mammalian liver aldolases (rat and rabbit).

Publisher

Canadian Science Publishing

Subject

General Medicine

Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. MOLAR ABSORPTIVITY AND A1%1cm VALUES FOR PROTEINS AT SELECTED WAVELENGTHS OF THE ULTRAVIOLET AND VISIBLE REGION. V*;International Journal of Peptide and Protein Research;2009-01-12

2. Enzymatic C-C Bond-Forming Reactions in Organic Synthesis;Current Organic Chemistry;2000-03-01

3. Enzymatic C-C bond formation in asymmetric synthesis;Topics in Current Chemistry;1996

4. C-C Bond Formation;Tetrahedron Organic Chemistry Series;1994

5. Studies on the structure of aldolase a from chicken muscle;Biochimica et Biophysica Acta (BBA) - Protein Structure;1981-02

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