-Whole mare (Mongolian and French breeds) casein was obtained from skim milk by isoelectric precipitation (pH 4.6) at 22 °C. In another series of experiments, equine caseins were fractionated after isoelectric precipitation at 4 °C, according to their sensitivity to temperature, on one hand, the pH of the resulting pellet was adjusted to 6.5 before centrifugation (45 000 g for 30 min) at 4 °C; on the resulting casein fraction which precipitated was named the cold precipitated (CP) fraction. On the other hand, the supernatant obtained from the centrifugation of skim milk at pH 4.6 and 4 °C was warmed to 30 °C before being centrifuged at 30 °C, 45 000 g, for 30 min. The resulting casein fraction which precipitated was named the thermally precipitated (TP) fraction. Equine caseins were then purified by high resolution gel chromatography on an anion-exchange column followed by reversed phase-high performance liquid chromatography. The casein fractions were analyzed by urea-and SDS-polyacrylamide gel electrophoresis, their amino acid compositions were determined and their first 15 N-terminal amino acids were sequenced. This analysis showed the presence of α slike caseins isolated from the CP fraction. α s1 -Like-casein showed 4 major double bands by electrofocusing with a pI range of 4.3-4.8. In the same conditions, α s2 -like casein showed 2 major bands with a pI range of 4.3-5.1. The TP fraction revealed the existence in equine milk of 6 subfractions of β-like caseins, occurring in the following ratios: 1:5:18:20:15:10, differing at least in their degree of phosphorylation (as shown also by the action of acid phosphatase). Since no evidence of the presence of κ-casein was found in equine milk, it is proposed that part of its functions in the milk of the Equidae could be assumed by the population of less phosphorylated β-caseins.
Summary -The composition of acid-precipitated caseins from ruminant Mongolian domestic animaIs was analyzed and a comparative study between camel (Camelus bactrianus) and dromedary (Camelus dromedarius) was realized. Acid-precipitated whole caseins were analyzed for ami no acid composition, separated by anion exchange chromatography and identified by alkaline urea-PAGE. Elution profiles and electrophoretic mobilities of the main components of yak and khainak caseins were nearly identical to their cow counterparts. However, the main part of a:;l-casein of yak was eluted in lower molarity in NaCI. Characterization by PAGE, ami no acid composition and N-terminal sequence of individual caseins from camel (Camelus bactrianus) indicated that milk of this ruminant contains dominantly a S1 -' a S2 -' and~-casein and small amounts of x-casein as is the case for the milk of dromedary (Camelus dromedarius).caseins / yak / khainak / camel Résumé -Caractérisation des caséines de ruminants de Mongolie: yak, khainak et chameau bactrien, La composition en acides aminés des caséines totales de deux ruminants de Mongolie (yak, khainak) a été déterminée. Les différentes caséines ont été séparées par chromatographie sur échangeur d'ions et analysées par électrophorèse en milieu urée et à pH alcalin. Les caséines des deux espèces étudiées ont un comportement voisin, proche de celui des caséines de vache. La seule différence notable réside dans le fait que chez le yak, la caséine a SI est éluée à une molarité inférieure à celle utilisée lors de la séparation des caséines de vache et de khainak. Une étude comparative a été réalisée entre le chameau (Camelus bactrianus) et le dromadaire (Camelus dromedarius). Ces deux espèces renferment principalement les caséines aS l' a S2 et B, dont la séquence N-terminale a été déterminée. La caséine K n'est que faiblement représentée.caséines / yak / khainak / camélidés
The composition of whey proteins from ruminant Mongolian domestic animals was analyzed and a comparative study between camel (Camelus bactrianus) and dromedary (Camelus dromedarius) was made. Whey proteins were separated by ion-exchange chromatography and identijied by polyacrylamide gel electrophoresis, amino acid composition and N-terminal sequence determination. The main components of wheys of yak and khainak were nearly identical with their bovine counterparts. Three different f o m of a-lactalbumin were isolated in the whey of Camelus bactrianus and two from Camelus dromedarius. As shown by classical biochemical and immunological studies, 0-lactoglobulin was absent from whey of both Camelus. Camel whey basic protein (CWBP), having no analogy with known milk and nonmilk proteins, was identifed in the whey of Camelus bactrianus and Camelus dromedarius and its N-terminal sequence was determined.
Various types of toxic xenobiotic and electrophilic compounds, which were formed from the glutathione S-transferases cell metabolism and the oxidation stress, are the group enzymes with detoxification roles that are involved in the metabolism phase II. During the GSTM1 and GSTT1 gene homozygous deletion, the above enzymes completely lose their activity and consequently somatic mutation is formed. Furthermore, it is considered that it might have increased the risk of cancer. Therefore, the research works which connected the GSTMI and GSTTI gene deletion with the cancer of kidney, lung, prostate, breast, stomach, esophagus, large and narrow intestines. In this study, two gene deletion distribution is detected for cancer patients. We collected the blood samples of 60 patients who have been diagnosed with cancer. The DNA was extracted and the GSTM1 and GSTT1 genes were amplified using multiplex PCR. According to our research, the above two gene deletion is predominant among patients who have cancer. The results showed that from the total 60 patients GSTM1 and GSTT1 both deletions, GSTM1 gene deletion - 35%, GSTM1 gene deletion - 25%, GSTT1 gene deletion - 26.7%, GSTM1 and GSTT1 both positive -13.3 %. Therefore, we think that in order to prevent tumor and cancer, these gene mutations must be revealed and it is important to bring the risky group under medical control and assist them in order to prevent them from this disease.
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