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A study of the hydrolysis of /?-casein-B by crystalline rennin or rennet extract at pH 6-5, using a disk electrophoresis technique, showed that 3 bonds in /ff-casein are appreciably more sensitive than the others to rennin proteolysis, and that these bonds are probably located near the C-terminus of the protein. The most susceptible bond is hydrolysed, at 10°C, about 200 times faster than any other bond, whilst at 37 °C it is hydrolysed 60 times faster. A study of the hydrolysis of this bond showed that its rate of hydrolysis at 37°C and pH 6-5 is decreased by either increased ionic strength or increased calcium ion concentration at constant ionic strength. Conformational changes in the substrate are probably responsible for these effects. 270

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