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Journal of Dairy Science Vol. 41 No. 2 317-318
© 1958 by American Dairy Science Association ®
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Isolation and Identification of {lambda}-Casein

John Long, Q. Van Winkle and I. A. Gould

Departments of Dairy Technology and Chemistry, The Ohio State University, Columbus

ABSTRACT

Waugh and von Hippel (8) have reported the presence of a casein component in cow's milk which they have named {kappa}-casein, and they have characterized {kappa}-casein in preparations which contained other casein components.1 Mc-Meekin, Groves, and Hipp (3)2 have described the use of calcium chloride for the isolation of {kappa}-casein from aqueous solutions of {alpha}-casein. A similar procedure, utilizing the difference in solubility exhibited by components of {alpha}-casein in the presence of calcium ions, has been employed in this laboratory (4) for the isolation of {kappa}-casein. We have found that the {kappa}-casein thus obtained is associated with a minor component which we have designated as {lambda}-casein. {lambda}-Casein has been isolated from the crude {kappa}-casein preparation by differential centrifugation, and characterized with respect to (a) phosphorus content, (b) stability to calcium ions, (c) reaction with rennet, and (d) sedimentation behavior. A comparison of these properties with those of {kappa}-casein (7) and {alpha}R-casein (defined later), indicates that {lambda}-casein was a separate and distinct protein component.







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Copyright © 1958 by the American Dairy Science Association ®.