Effect of Ketosteril and Low Protein Diet on Nutritional Status and Renal Function in Patients with Chronic Kidney Disease / 中国慢性病预防与控制

Objective To investigate the effect of Ketosteril and low protein diet on nutritional status and renal function in patients with chronic kidney disease (CKD). Methods 60 patients with CKD were divided into two groups randomly. The patients were treated with low-protein diet (0.6 g?kg-1?d-1) in control group while the patients was treated with Ketosteril (0.2 g?kg-1?d-1) and low-protein diet (0.6 g?kg-1?d-1) in the test group. The intervention period lasted for 3 months. The body weight, MAC, MAMC and the serum ALB, PA, Tf, BUN and Cr concentrations in the patients were measured. Results Compared with the control group, the body weight, MAC, MAMC were significantly increased in the test group; the serum ALB, PA ,Tf, BUN and Cr concentrations were also improved. Conclusion Combination of Ketosteril and low-protein diet can improve the nutritional status and the kidney function.

Isolation and identification of yolk proteins in Indian major carp, Labeo rohita.

Two yolk proteins (YP1 and YP2) from the ovaries of Indian major carp, Labeo rohita were isolated by gel filtration and partially characterized by the use of hydroxyapatite ultrogel column in conjunction with native PAGE. On native PAGE YP1 gave a single protein band, whereas YP2 of gel filtration revealed the contamination of YP1, which was removed by adsorption chromatography on hydroxyapatite ultrogel and then the YP2 was the purified one as judged by electrophoresis. Both YP1 and YP2 also stained for lipid and contained alkali-labile phosphorus. Therefore, both yolk proteins were lipophosphoprotein. The molecular weights of YP1 and YP2 were 620 kDa and 225 kDa respectively as determined by gel filtration on Sepharose 4B. When YP1 and YP2 were compared in relation to some physicochemical characteristics with yolk proteins of other oviparous vertebrates including fish, they were lipovitellin like. Antiserum to YP2 crossreacted with YP2 and vitellogenin suggesting that YP2 was the cleaved product of vitellogenin. Anti-YP2 antiserum was not crossreacted with native YP1, whereas reduced and/or denatured YP1 was crossreacted indicating the presence of antigenic determinants in the inner core region of YP1 polypeptide.