Correlation between Molecular Weight Distribution of Oligo-L-methionine Prepared by, Papain-catalyzed Polymerization and Its Supplementary Effect in a Low Protein Diet

1992 ◽  
Vol 56 (11) ◽  
pp. 1884-1885 ◽  
Author(s):  
Takanori Kasal ◽  
Tomoyuki Tanaka ◽  
Shuhachi Kiriyama
Keyword(s):  
Molecular Weight ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Low Protein ◽  
Catalyzed Polymerization

Hepatic Ultrastructure Changes Induced by Lithocholic Acid

1967 ◽  
Vol 25 ◽  
pp. 162-163 ◽  
Author(s):  
F. G. Zaki
Keyword(s):  
Endoplasmic Reticulum ◽  
Lithocholic Acid ◽  
Smooth Endoplasmic Reticulum ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Electron Microscopic ◽  
Hydropic Degeneration ◽  
Hepatic Cells ◽  
Low Protein ◽  
Microscopic Studies

Addition of lithocholic acid (LCA), a naturally occurring bile acid in mammals, to a low protein diet fed to rats induced marked inflammatory reaction in the hepatic cells followed by hydropic degeneration and ductular cell proliferation. These changes were accompanied by dilatation and hyperplasia of the common bile duct and formation of “gallstones”. All these changes were reversible when LCA was withdrawn from the low protein diet except for the hardened gallstones which persisted.Electron microscopic studies revealed marked alterations in the hepatic cells. Early changes included disorganization, fragmentation of the rough endoplasmic reticulum and detachment of its ribosomes. Free ribosomes, either singly or arranged in small clusters were frequently seen in most of the hepatic cells. Vesiculation of the smooth endoplasmic reticulum was often encountered as early as one week after the administration of LCA (Fig. 1).

Extraction and Partial Purification of Protease from Bilimbi (Averrhoa bilimbi L.)

2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe
Keyword(s):  
Molecular Weight ◽  
Protein Content ◽  
Ammonium Sulfate ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Protease Activity ◽  
Protein Concentration ◽  
Temperature Stability ◽  
Partial Purification ◽  
Ammonium Sulfate Precipitation

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 

Sign in / Sign up

Export Citation Format

Share Document