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Effect of Deficient and Excess Dietary Vitamin B-6 on Amino Transaminase and Glycogen Phosphorylase Activity and Pyridoxal Phosphate Content in Two Muscles from Postpubertal Gilts

Department of Animal Science, University of Illinois at Urbana-Champaign, Urbana, IL 61801

Postpubertal gilts averaging 111 kg and gaining 2.7 kg/wk were fed daily 1.9 kg/d of a diet providing 0.45, 2.1 or 83 mg of vitamin B-6/d. An additional group of animals were fed the high vitamin B-6 diet providing 83 mg of vitamin B-6/d for the initial 57 d of the experiment and then switched to 0.45 mg of vitamin B-6/d for the remainder of the 121-d experiment (61 gilts total). On d 0, 57 and 121, animals from each treatment were killed, and samples of the semitendinosus (ST) and semimembranosus (SM) were removed. Glutamic-oxaloacetic transaminase (GOT), glutamic-pyruvic transaminase (GPT), glycogen phosphorylase and pyridoxal phosphate (PLP) were measured in muscle tissues. The erythrocyte GOT activity coefficient indicated that gilts consuming 0.45 or 2.1 mg of vitamin B-6/d developed a vitamin B-6 deficiency. A vitamin B-6 deficiency resulted in the loss of whole-muscle transaminase activity (enzyme activity x muscle weight) with little effect on whole-muscle total phosphorylase or total PLP content. Excess dietary vitamin B-6 increased whole-muscle total PLP and total phosphorylase content with small decreases in whole-muscle transaminase. Under these conditions, muscle tissue acts as a nonmobile reservoir of PLP. Sixty to 95% of muscle PLP was bound to muscle glycogen phosphorylase.

KEY WORDS: • vitamin B-6 • muscle • transaminase • phosphorylase

¹ Present address: Feed Specialties Co., 1877 N.E. 58th Avenue, Des Moines, IA 50313.

² Send reprint requests to P. J. Bechtel, Muscle Biology Laboratory, 1503 South Maryland Drive, University of Illinois, Urbana, IL 61801.

Manuscript received 31 August 1984. Revision accepted 23 May 1985.