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Diluters for Bovine Semen. III. Effect of Lactenin and of Lactoperoxidase upon Spermatozoan Livability¹

Dairy Cattle Breeding Research Center, Department of Dairy Husbandry, The Pennsylvania State University, State College

ABSTRACT

The fractionation of milk proteins by Thacker et al. (14) indicated that the factor(s) present in unheated milk which are toxic to bovine spermatozoa are associated with the albumin-containing fractions. However, much of the activity was lost during the fractionation procedure and none of the fractions retained more than a portion of the toxicity of the source material. The heat lability, nondialyzability and loss of activity with salt fractionation suggested that the factor might be enzymatic in nature. Most of the known enzymes in milk are inactivated by heating to 92° C. for 10 minutes, although lactoperoxidase is a notable exception (9). Another approach to the problem of identifying the spermicidal factor(s) is suggested by the similarity between the characteristics of the spermicidal factor (s) of unheated milk (5, 13, 14) and lactenin (1, 2, 6, 7, 8, 17, 18), an antistreptococcal substance found in milk which was originally prepared in concentrated form by Jones and Simms (7).

¹ Approved for publication by The Pennsylvania Agricultural Experiment Station on April 27, 1954 as Journal Article No. 1873.

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