Report to the Local Government Board upon the "biological properties" of milk, both of the human species, and of cows, considered in special relation to the feeding of infants / by Janet E. Lane-Claypon.

  • Lane-Claypon, Janet E.
Date:
1913
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Licence: In copyright

Credit: Report to the Local Government Board upon the "biological properties" of milk, both of the human species, and of cows, considered in special relation to the feeding of infants / by Janet E. Lane-Claypon. Source: Wellcome Collection.

    16/100 (page 14)
    Kastle and Porcli('^‘’) (1908) fomid the results of tlie peroxidase reaction very uncertain with human milk, even with the addition of tlieir sensitiser trikresol; the colostrnl sta^-e appeared to have, as a whole, greater activity than the later milk. Tlie peroxidase reaction lias been found xmsitive in goats’ milk, by Spolverini(^^°) (1902), Luzzati and Biolchini('^) (1902), E.audnitz(^'^'”^) (1898), Grimmer(’^^’) (1910), Harden and Lane- Claypon('''’) (1912), and by Weber(^'^) (1910), who worked with colostrum only. It was positive in sheeps’ milk. {Cj). Raudnitz, Grimmer, and AVeber.) Raudnitz (1898) found the reaction negative in the ordinary milk of the horse, dog, ass, and rabbit, but positive in the colo- strum of these animals. Spolverini (1902) found it weakly positive in the milk of dogs and asses, and Grimmer found it negative in the milk of the horse and pig. Reviewing the work described in sections 5 and 6, it appears that peroxidase is constantly present in the milk of cows, and only inconstantly present in human milk. There is no reason to suppose that it is bacterial in origin. Comparing the work of Weber, Giffhorn, Grimmer, Spolverini,. and Marfan and Gillet, it appears that peroxidase is derived from cellular elements, and at any rate in great part, from the leucocytes. 2.—'Catalase. The name catalase is now very widely, if not universally, applied to the ferment, generally found in both animal and vege- table tissues, having the property of splitting hydrogen peroxide into water and oxygen, with the formation of molecular or inactive oxygen, according to the equation— 2H2O2 = 2H2O + O^. The name of this ferment has been the subject of considerable discussion, and it has not infrequently been called superoxydase; in this report, however, the more generally accepted nomen- clature will be followed throughout, and the ferment will be termed catalase, even in dealing with papers by authors who prefer the other term. The literature dealing with the presence of this body in the milk of various animals is extremely voluminous, and much of it does not present sufficient interest for it to be necessary to deal with it in detail. Many of the papers are concerned with the attempt to find a relationship between the catalase content and the purity or otherwise of the milk; this aspect will be referred to somewhat briefly, as it does not come strictly within the scope of the present investigation. On the Vves^ence of Catalase in Cows^ Milk. Tlie existence of this ferment was known for manv vears before « «. its presence in milk was detected. In 1882 (^^' ^°), Becanip and Bert and Regnard(^^), showed that tliis property was common to extracts of practically all the