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Some Characteristics of the Glyco-Macropeptide of Casein—A Product of the Primary Rennin Action¹

Department of Dairy, Food Technology Program, Michigan Agricultural Experiment Station, East Lansing

ABSTRACT

The primary action of rennin on casein and the concurrent release of nonproteolytic NPN have been the subject of recent investigations. Recently, Wake (5) showed that -casein, the calcium-insensitive protective colloid of the -casein complex, was the substrate for the primary action of rennin. Alais (1) isolated two groups of peptides from the NPN fraction. One group, soluble in 2% TCA, was found to be electrophoretically heterogeneous and contained a major component which constituted 90% of the total 12% TCA-soluble constituents. The electrophoretic mobility of this component was reported at 7 to 8 cm.² v.^–1 sec.^–1 x 10^–5 in veronal buffer at pH 8.6. Nitschmann et al. (4) found this component, ranging in molecular weight between 6,000 and 8,000, to be rich in carbohydrate and, consequently, the term glyco-macropeptide was used to describe the peptide.

The objective of our studies has been to elucidate the composition and physical characteristics of this electrophoretically homogeneous glyco-macropeptide.

¹ Michigan Agricultural Experiment Station Journal Article No. 2452.