Search PubMedSearch

Biomedical subjects

G Miranda

Publications and source records attributed to G Miranda.

4 recordsLinked to original sources

Milking of cows in late pregnancy: milk production during this period and during the succeeding lactation.

Fifteen lactating cows were milked throughout pregnancy, and the effects on milk performance were studied during this period and during the succeeding lactation, relative to 11 conventionally managed cows (2 months dry before calving) as controls. During the last 2 months of pregnancy, only nine cows did not dry off spontaneously. Protein and fat concentrations in milk increased rapidly, but the concentration of lactose, corrected for milk yield, did not change. The ratios of individual caseins to total protein decreased with the quantity of milk produced, but only for yields below approximately 6 kg/d. The relative proportion of kappa-casein tended to decrease in the last milkings. During the succeeding lactation (first 15 weeks after calving and first 6 weeks of grazing) continuously milked cows yielded 4 kg milk/d less than the cows of the other group. The protein content of their milk was higher (2-3 g/kg depending on the period) than that of the control group, and the lactose content tended (P less than 0.10) to be lower. Changes in the relative proportions of nitrogenous fractions with time were not different in the two groups. Differences between the two groups in the concentration of protein in milk, and in the concentration of glucose and non-esterified fatty acids in the plasma, suggest a better energy balance for the continuously milked cows during the succeeding lactation.

Animal Nutritional Physiological Phenomena

Hydrolysis of beta-casein by gastric proteases. I. Comparison of proteolytic action of bovine chymosin and pepsin A.

Hydrolysis of beta A2-casein by bovine chymosin and pepsin A was performed in order to compare the hydrolysis of the two enzymes on this protein. Different conditions have been tested: pH 5.5 for 116h and pH 3.5 for 7 h [E/S = 1/100 (w/w)] for chymosin. pH 3.0 for 24 h [E/S = 1/1000 (w/w)] for pepsin A. Under these conditions 17 peptides were obtained after the action of chymosin and 23 after the action of pepsin A. They corresponded respectively to the cleavage of 14 and 15 peptide bonds for chymosin and pepsin A. However, six of the peptide bonds were only hydrolyzed by chymosin and seven other bonds only by pepsin A. Our results showed a preferential splitting at the Leu-X, Ser-X, and Trp-X bonds for chymosin and Leu-X, Met-X, and Thr-X, for pepsin A. Some of the identified peptides contained sequences with possible physiological roles.

Amino Acid Sequence