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The tertiary phase of rennin action on αs- and β-caseins

Published online by Cambridge University Press:  01 June 2009

A. M. El-Negoumy
A. M. El-Negoumy
Affiliation:
Agricultural Products Utilization Laboratory, Biochemistry Section, Department of Animal and Range Sciences, Montana State University, Bozeman, U.S.A.
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Summary

Casein, whole αs-casein and β-casein were incubated for 3 and 14 h with crystalline rennin, at pH 6·60 and 36 °C, both in phosphate buffer and in milk dialysate. Products obtained from both systems, comprising 30–83% calciumsensitive (Cas) components, gave similar patterns on starch gel electrophoresis. Whole casein and whole αs-casein were not so soluble in milk dialysate as in phosphate buffer. No significant differences in composition were observed between the Cas and the calcium-insensitive (Ca1) products from the same source.

The αs1-component of the Cas product from rennin-treated whole αs-casein had faster gel mobility in comparison to the αs1-component in the Cas product from untreated whole αs-casein. Also, αs1-casein yielded one faster-moving degradation product, while αs2,3,4 appeared unaltered after 14h. The Cas product of rennintreated β-casein also had faster mobility than untreated β-casein and yielded one faster degradation product and several minor ones of slower mobility. Arginine was the only N-terminal amino acid found in the Cas product of both rennin-treated and untreated αs - and β-caseins. The arginine content increased from 3·48 and 4·98 moles/105g to 5·12 and 6·38 moles/105g in the Cas products from rennin-treated β-and αs-caseins, respectively.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 3 , October 1970 , pp. 437 - 444
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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References

REFERENCES

Alais, C., Mocquot, G., Nitschmann, H. & Zahler, P. (1953). Helv. chim. Acta 36, 1955.Google Scholar
Block, R. J. (1960). In A Laboratory Manual of Analytical Methods of Protein Chemistry (Including Polypeptides) 2, 15–16 (Eds Alexander, P. and Block, R. J.). New York: Pergamon Press.Google Scholar
Cerbulis, J., Custer, J. H. & Zittle, C. A. (1959). Archs Biochem. Biophys. 84, 517.Google Scholar
Cerbulis, J., Custer, J. H. & Zittle, C. A. (1960). J. Dairy Sci. 43, 1725.CrossRefGoogle Scholar
Cherbuliez, E. & Baudet, P. (1950). Helv. chim. Acta 33, 1673.Google Scholar
El-Negoumy, A. M. (1966). J. Dairy Sci. 49, 1461.CrossRefGoogle Scholar
El-Negoumy, A. M. (1968). J. Dairy Sci. 51, 1013.Google Scholar
Fraenkel-Conrat, H., Harris, J. F. & Levy, A. L. (1955). Meth. biochem. Analysis 2, 359.Google Scholar
Garnier, J., Ribadeau-, B. & Mocquot, G. (1964). J. Dairy Res. 31, 131.Google Scholar
Hagberg, E. C. & Sullivan, R. A. (1953). J. Dairy Sci. 36, 569.Google Scholar
Kalan, E. B., Thompson, M. P., Greenberg, R. & Pepper, L. (1965). J. Dairy Sci. 48, 884.CrossRefGoogle Scholar
Lahav, B. & Babad, Y. (1964). J. Dairy Res. 31, 31.CrossRefGoogle Scholar
Levy, A. L. (1954). Nature, Lond. 174, 126.Google Scholar
Lindqvist, B. (1963). Dairy Sci. Abstr. 25, 299.Google Scholar
Lindqvist, B. & Storgårds, T. (1959). Acta chem. scand. 13, 1839.Google Scholar
Lindqvist, B. & Storgårds, T. (1960). Acta chem. scand. 14, 757.Google Scholar
Lindqvist, B. & Storgårds, T. (1962). 16th Int. Dairy Congr., Copenhagen B, 665.Google Scholar
McMeekin, T. L., Hipp, N. J. & Groves, M. L. (1959). Archs Biochem. Biophys. 83, 35.CrossRefGoogle Scholar
Manson, W. (1961). Archs Biochem. Biophys. 95, 336.Google Scholar
Masayoshi, O. (1956). 14th Int. Dairy Congr., Rome 2 (2), 379.Google Scholar
Nitschmann, Hs. & Keller, W. (1955). Helv. chim. Acta 38, 942.Google Scholar
Nitschmann, Hs. & Lehmann, W. (1947). Experientia 3, 153.Google Scholar
Ribadeau Dumas, B. & Alais, C. (1961). Bull. Soc. Chim. biol. 43, 377.Google Scholar
Rose, D., Davies, D. T. & Yaguchi, M. (1969). J. Dairy Sci. 52, 8.CrossRefGoogle Scholar
Schmidt, D. G. & Payens, T. A. J. (1963). Biochim. biophys. Acta 78, 492.Google Scholar
Tsugo, T. & Yamauchi, K. (1956). 14th Int. Dairy Congr., Rome 2 (2), 588.Google Scholar
Warren, L. (1959). J. biol. Chem. 234, 1971.CrossRefGoogle Scholar
Yaguchi, M., Davies, D. T. & Kim, Y. K. (1968). J. Dairy Sci. 51, 473.CrossRefGoogle Scholar