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Open AccessJournal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

Klaus Weber, +1 more
- 25 Aug 1969 - 
- Vol. 244, Iss: 16, pp 4406-4412
TLDR
The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
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This article is published in Journal of Biological Chemistry.The article was published on 1969-08-25 and is currently open access. It has received 19381 citations till now. The article focuses on the topics: Polyacrylamide gel electrophoresis & Sodium dodecyl sulfate.

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Citations
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.

TL;DR: The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related.
Journal ArticleDOI

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

TL;DR: A rapid and convenient method for peptide mapping of proteins has been developed that involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis.
Journal ArticleDOI

The Regulation of Rabbit Skeletal Muscle Contraction I. BIOCHEMICAL STUDIES OF THE INTERACTION OF THE TROPOMYOSIN-TROPONIN COMPLEX WITH ACTIN AND THE PROTEOLYTIC FRAGMENTS OF MYOSIN

TL;DR: Actin purified by a new, simple, and rapid purification procedure activated the ATPase activity of both heavy meromyosin and Subfragment 1 of heavy mercyosin, and this activation was not inhibited by the removal of Ca2+.
References
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Journal ArticleDOI

Disc electrophoresis – ii method and application to human serum proteins*

TL;DR: The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.
Journal ArticleDOI

Disc electrophoresis-i background and theory*

TL;DR: Some mechanisms that provide a rationale for the resolution afforded by zone electrophoresis in many gels will be detailed; the theory of some new modifications of zone electophoresis that have been designed to take maximum advantage of these mechanisms will be developed.
Journal ArticleDOI

The oxidation of ribonuclease with performic acid.

TL;DR: The present investigation was undertaken to determine quantitatively the stability of each of the amino acid residues in the ribonuclease molecule under the conditions employed for the oxidation of the cystine sulfur bridges.
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