Separation methods for milk proteins on polyacrylamide gel electrophoresis: Critical analysis and options for better resolution.
KRISHI: Publication and Data Inventory Repository
View Archive InfoField | Value | |
Title |
Separation methods for milk proteins on polyacrylamide gel electrophoresis: Critical analysis and options for better resolution.
Not Available |
|
Creator |
Sharma, N.; Sharma, R.; Rajput, Y.S.; Mann, B.; Singh, R. and Gandhi, K.
|
|
Subject |
polyacrylamide gel electrophoresis
|
|
Description |
Not Available
Over the years, a number of methodological variations in polyacrylamide gel electrophoresis (PAGE) have been attempted for the separation of milk proteins. Caseins are similar in size and differ very little in net charge from each other. Also, in heated milk, k-casein not only complexes with whey proteins but also undergoes self-polymerisation. These cause problems in the resolution of milk proteins and encouraged researchers to modify PAGE. Seven different types of PAGE, i.e., native-PAGE, urea-PAGE, reducing sodium dodecyl sulphate (SDS)-PAGE, non-reducing-SDS-PAGE, urea-SDS-PAGE, tricine-PAGE, and two dimensional electrophoresis (2DE), are reviewed with particular emphasis on the pattern of milk pro tein electrophoretograms, merits, demerits and applications. Although the literature suggests that SDS PAGE is increasingly used for separating milk proteins, other forms of PAGE have their own advantage. This review can act as a quick screening aid for researchers in selecting an appropriate type of PAGE for the separation of milk proteins for different purposes. Not Available |
|
Date |
2021-08-26T08:36:46Z
2021-08-26T08:36:46Z 2021-03-01 |
|
Type |
Research Paper
|
|
Identifier |
Not Available
Not Available http://krishi.icar.gov.in/jspui/handle/123456789/60786 |
|
Language |
English
|
|
Relation |
Not Available;
|
|
Publisher |
Elsevier
|
|