Clinical evaluations of a new prostaglandin analog in pigs: 1. Control of parturition and of the MMA-syndrome.
In two field trials, the parturition inducing and MMA preventing effects of the prostaglandin F(2alpha) analog (PGFA), K 11941, were explored. In trial 1, 100 sows were treated with 2 mg and 30 with 3 mg of K 11941 i.m. on day 112 of gestation; 125 sows treated on day 112 with 175 mcg cloprostenol (Planate, ICI) served as positive controls, and 248 sows treated with saline on day 112 of gestation were used as negative controls. Both PGF analogs were equally effective in inducing early parturiton: 84.6% and 83.2% of the sows had farrowed between 20 and 30 hours after treatment. Both treatments reduced stillbirth rate and piglet losses during the first 10 days of life, and lowered the incidence of MMA significantly (6.2 and 5.6% vs 27.3 and 24.2%; p<.001). In a second trial, parturitions were induced in four groups of 60 sows each with 2 mg K 11941, housed in farms with either a chronic high incidence of MMA (A: 45 to 65% or only a seasonal rise in MMA during summer (B: 10 to 50%). Groups were treated either in April/May or August/September; 240 salinetreated, control sows were used. K 11941-induced parturition reduced MMA incidence in farm A during both seasons and prevented the summer rise in farm B (p<.01). Fertility after weaning was impaired in herds with an increased incidence of MMA.
Induced parturition in swine with prostaglandin F2α.
豚において妊娠の110,112,113,114日(それぞれ分娩予定日の4,2,1,0日前)にPGF2α10mgの単一筋肉注射による分娩誘起を試みた。その結果,処置後23~38時間以内に分娩を開始することを認めた。
On the fractionation of β-lactoglobulin and α-lactalbumin
Abstract Existing methods for the preparation of α-lactalbumin and β-lactoglobulin are examined critically. It is proposed that the most satisfactory method for the preparation of the whey protein fraction from bovine milk is (NH 4 ) 2 SO 4 fractionation. A number of new gentle procedures for the fractionation of the whey proteins are compared with some existing methods. The distribution of total protein at various stages is determined by total Kjeldahl nitrogen and the kind of protein by starch-gel electrophoresis. The effect of variables, such as pH, salt concentration and temperature on the separation of α-lactalbumin and serum albumin from β-lactoglobulin is studied. Differences in the behavior ( e.g. solubility) of genetic variants of β-lactoglobulin are noted. The solubility of each of the major whey proteins, under similar conditions to those used in the fractionation, is compared with its solubility in the whey protein mixture. The understanding gained of factors important in the fractionation is used in recommending new procedures for α-lactalbumin and β-lactoglobulin isolation.