Development of an SDS-gel electrophoresis method on SU-8 microchips for protein separation with LIF detection: Application to the analysis of whey proteins

2013 ◽  
Vol 36 (15) ◽  
pp. 2530-2537 ◽  
Author(s):  
Maria del Mar Barrios-Romero ◽  
Agustín G. Crevillén ◽  
José Carlos Diez-Masa
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Whey Proteins ◽  
Electrophoresis Method

Proteolysis of caseins and the proteose-peptone fraction of bovine milk

1983 ◽  
Vol 50 (3) ◽  
pp. 275-290 ◽  
Author(s):  
Anthony T. Andrews ◽  
Efstathios Alichanidis
Keyword(s):  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Major Product ◽  
Natural Course ◽  
Pasteurized Milk ◽  
Proteose Peptone ◽  
History Of

SummaryThe proteolysis of highly purified samples of αs1-, αs2-, β-and κ-caseins by porcine plasmin and by bovine plasminogen with urokinase has been examined principally by gel electrophoresis. The resulting peptide band patterns were compared with those of total proteose-peptone (TPP) samples prepared from fresh and stored raw and pasteurized milk, and also with those obtained during the natural course of proteolysis by indigenous enzymes in milk during storage. TPP was found to contain at least 38 components detectable by a single electrophoresis run. Apart from residual traces of whey proteins and intact caseins nearly all of these components were fragments of caseins produced by indigenous plasmin, with products from the breakdown of αs1- and β-casein predominating. Over 90 % of TPP has been accounted for in this way. A fragment consisting of residues 29–105 of β-casein was isolated and characterized from both stored milk and from plasmin digests of β-casein. This fragment was a relatively major product of the natural proteolysis occurring during storage of milk, but contrary to a report in the literature it was not the same as proteose-peptone component 8-slow. Since many of the components of TPP resulted from proteolysis, the composition of TPP was found to vary according to the time and temperature of storage of the milk from which it was prepared. Thus, while the proteose-peptone fraction of milk can easily be defined operationally it cannot be rigorously defined in terms of its composition unless the history of the milk is also defined.

Influence of dietary proteins on rennin and pepsin content of preruminant calf vell

1974 ◽  
Vol 41 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Pascaline Garnot ◽  
E. Valles ◽  
J.-L. Thapon ◽  
R. Toullec ◽  
R. Tomassone ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Deae Cellulose ◽  
Milk Proteins ◽  
Total Activity ◽  
Separate Experiment ◽  
Dietary Proteins ◽  
Constant Weight ◽  
Cellulose Column ◽  
Qualitative Analyses

SummaryStudies were undertaken to determine the influence of dietary proteins on the rennin and pepsin contents of preruminant calf vell. Three groups of 12 Friesian calves were each fed either milk proteins, whey proteins or a 50:50 mixture of these 2 diets. They were slaughtered at a constant weight of 150kg and their vells collected and dried. Another group of vells was obtained from 8 animals that had been fed milk proteins in a separate experiment. The extraction of the abomasal enzymes was carried out at acid pH, and the extracts were quantitatively analysed for rennin and pepsin by DEAE-cellulose column chromatography. Qualitative analyses were also performed by agarose-acrylamide gel electrophoresis. The only enzymes observed using this last method were rennin and bovine pepsin II. Statistical analysis of the quantitative enzyme determinations indicated a trend for the vells from calves fed diets containing casein to be richer in total activity and in rennin, while the level of pepsin remained approximately constant. It seems that casein may induce the secretion of rennin. However, further experiments will be necessary to confirm this. Important differences were observed between the 2 groups of veils from calves given the same diet, but grown in slightly different conditions.

scholarly journals Development of a highly sensitive three-dimensional gel electrophoresis method for characterization of monoclonal protein heterogeneity

2013 ◽  
Vol 438 (2) ◽  
pp. 117-123 ◽  
Author(s):  
Keiichi Nakano ◽  
Shogo Tamura ◽  
Kohei Otuka ◽  
Noriyasu Niizeki ◽  
Masahiko Shigemura ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Three Dimensional ◽  
Monoclonal Protein ◽  
Highly Sensitive ◽  
Electrophoresis Method

Study on Degradation of Radix Isatidis Polypeptide in Artificial Gastrointestinal Environment

2014 ◽  
Vol 989-994 ◽  
pp. 1020-1024
Author(s):  
Nan Nan ◽  
Xi Jing Liu
Keyword(s):  
Gel Electrophoresis ◽  
Free Amino ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Radix Isatidis ◽  
Sds Page ◽  
Electrophoresis Method ◽  
Amino Acid Levels ◽  
Different Molecular Weight

Radix Isatidis is a traditional Chinese medicine for treatment of influenza and inflammation in China. In this paper, in order to study the degradation situation of Radix Isatidis polypeptide in artificial gastrointestinal environment, the SDS-PAGE (Sodium dodecyl sulfate-polyacrylamide gel electrophoresis) method was used to detect the degradation of Radix Isatidis polypeptide in artificial intestinal juice and gastric juice, and it showed that Radix Isatidis peptides could be degradated to different degrees. HPLC (High Performance Liquid Chromatography) was used to determine the change of peptides degradation, and it indicated that free amino acid levels did not change significantly. The result after degradation was also detected by BCA method, and it showed that there were still a large number of polypeptides in the liquid. From this experiment we can come to this conclusion that Radix Isatidis polypeptides in artificial gastrointestinal juice mostly degraded into a series of different molecular weight peptides.

A new quantitative gel electrophoresis method with image-based detection for the determination of food dyes and metallic ions

Talanta ◽  
2021 ◽  
Vol 221 ◽  
pp. 121602
Author(s):  
Gerson Francisco da Silva Neto ◽  
Maria Luíza de Andrade Rodrigues ◽  
Alexandre Fonseca
Keyword(s):  
Gel Electrophoresis ◽  
Metallic Ions ◽  
Food Dyes ◽  
Electrophoresis Method
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