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Observations on the proteins of pasturage. Phosphorus and protoplasm

Published online by Cambridge University Press:  27 March 2009

F. W. Foreman
F. W. Foreman
Affiliation:
School of Agriculture, Cambridge University
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Extract

1. Studies lead to the conclusion that Chibnall-preparations of pasturage proteins, in spite of their small amounts of carbohydrate impurity, may yet yield, on hydrolysis by mineral acids, practically the right amounts even of most of those amino-acids which are adversely affected by carbohydrates to some extent when tested singly under the conditions.

2. Preparations made in another way after treating the pasturage with ether as in the original Chibnall-method showed features of interest in the problem of attaining very pure proteins now much needed for purposes of comparison.

3. A new method is introduced by which it is possible to compare what may be extracted from the protoplasm of fresh unpulverized pasturages with the composition of the natural saps on a unit weight basis.

4. Production and breakdown of protoplasmic protein in perennial rye-grass during growth consistently appeared related to variations in the content of “nitrogen” and phosphates in the saps and the supplies of “nitrogen” and phosphates from the soil.

Type
Research Article
Information
The Journal of Agricultural Science , Volume 28 , Issue 1 , January 1938 , pp. 135 - 173
Copyright
Copyright © Cambridge University Press 1938

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References

REFERENCES

Ames, and Boltz, (1912). Bull. Ohio agric. Exp. Sta. No. 247.Google Scholar
Browne, (1912). A Handbook of Sugar Analysis, 1st ed. p. 452. London.Google Scholar
Chibnall, (1923). J. biol. Chem. 55, 333.CrossRefGoogle Scholar
Chibnall, (1924). J. biol. Chem. 61, 303.CrossRefGoogle Scholar
Chibnall, , Miller, , Hall, & Westall, (1933). Biochem. J. 27, 1879.Google Scholar
Clarke, and Schryver, (1917). Biochem. J. 11, 323.CrossRefGoogle Scholar
Csonka, (1935). J. biol. Chem. 109, 703.CrossRefGoogle Scholar
Cunningham, and Dorée, (1914). Biochem. J. 8, 444.CrossRefGoogle Scholar
Foreman, (1920). Biochem. J. 14, 451.CrossRefGoogle Scholar
Foreman, (1928). Biochem. J. 22, 208.CrossRefGoogle Scholar
Gortner, (1916). J. biol. Chem. 26, 177.CrossRefGoogle Scholar
Hillebrand, and Lundell, (1929). Applied Inorganic Analysis, p. 557. London.Google Scholar
Hutchison, and Mottram, (1933). Food and the Principles of Dietetics, 7th ed. p. 297. London.Google Scholar
Jones, (1914). Nucleic Acids. Monographs on Biochemistry. London.Google Scholar
Maillard, (1912). C.R. Acad. Sci., Paris, 154, 66.Google Scholar
McCance, and Shipp, (1933). Spec. Rep. Ser. med. Res. Coun., Lond., 187, 35.Google Scholar
Miller, (1935). Biochem. J. 29, 2348.CrossRefGoogle Scholar
Miller, and Chibnall, (1932). Biochem. J. 26, 392.CrossRefGoogle Scholar
Plimmer, (1917). The Chemical Constitution of the Proteins. Part I. Analysis, 3rd ed. (Monographs on Biochemistry.) London.Google Scholar
Pollard, and Chibnall, (1934). Biochem. J. 28, 326.CrossRefGoogle Scholar
Roxas, (1916). J. biol. Chem. 27, 71.CrossRefGoogle Scholar
Seifriz, (1936). Protoplasm, 1st ed. New York and London.Google Scholar
Williams, (1917). J. agric. Sci. 8, 182.CrossRefGoogle Scholar