Alterations in rat serum proteins in relation to dietary proteins and B vitamins. I. Studies with growing rats

Mulgaonkar, Anand G. ; Sreenivasan, A. (1959) Alterations in rat serum proteins in relation to dietary proteins and B vitamins. I. Studies with growing rats Proceedings of the Indian Academy of Sciences, Section B, 49 (6). pp. 408-419. ISSN 0370-0097

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Official URL: http://www.ias.ac.in/j_archive/procb/49/6/408-419/...

Related URL: http://dx.doi.org/10.1007/BF03053877

Abstract

The alterations in rat serum proteins resulting from (i) variations in dietary protein quality and level, (ii) minimal intakes of B vitamins and (iii) single and combined deficiencies of vitamin B12 and folic acid have been studied with egg albumin, casein and peanut protein diets at 10 and 18 per cent. protein levels. Protein quality chiefly influences serum concentrations of albumin and α1-globulin, the effects on other fractions being variable. Protein level affects serum levels of albumin, α1-globulin and α2-globulin. The effects due to these dietary variables are interdependent. Variations in dietary protein quality do not alter the relative distribution of serum protein fractions. Changes in protein level cause shifts in the relative distribution of globulins, the albumin-globulin ratio remaining unaltered. The nature and extent of changes in serum protein profile due to vitamin insufficiencies or deficiencies are also influenced, qualitatively and quantitatively, by dietary amino acids. With minimal intakes of B vitamins γ-globulin is chiefly reduced, but other fractions, particularly α1-globulin, may also be affected. In a combined deficiency of vitamin B12 and folic acid a common reduction in γ-globulin is variably attended by reductions in albumin and in α1- and β-globulins. In single vitamin B12 deficiency, the changes are confined to albumin, α1-globulin and α2-globulin fractions, whereas single folic acid deficiency chiefly affects γ-globulin with variable effects on albumin and β-globulin fractions.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
ID Code:35794
Deposited On:21 Apr 2011 12:01
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