scholarly journals Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure.

1975 ◽  
Vol 142 (3) ◽  
pp. 664-672 ◽  
Author(s):  
J D Capra ◽  
E S Vitetta ◽  
J Klein
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Disulfide Bridge ◽  
Subunit Structure ◽  
Polyacrylamide Gels ◽  
Specific Antisera ◽  
Dodecyl Sulfate

The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of beta2-microglobulin.

scholarly journals ISOLATION AND REACTIVATION OF THE AXOSTYLE

1973 ◽  
Vol 56 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Mark S. Mooseker ◽  
Lewis G. Tilney
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Atpase Activity ◽  
Adenosine Triphosphate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gels ◽  
Molecular Weights ◽  
Dodecyl Sulfate ◽  
Cilia And Flagella ◽  
Triton X

The contractile axostyle is a ribbon-shaped organelle present in certain species of flagellates found in the hindgut of wood eating insects. This organelle propagates an undulatory wave whose motion, like flagella and cilia, is related to microtubules. Unlike the axoneme of cilia and flagella, however, the axostyle is composed of singlet microtubules linked together in parallel rows. Axostyles were isolated from Cryptocercus gut protozoa with Triton X-100. Normal motility of the isolated axostyle could be restored with adenosine triphosphate (ATP); the specific conditions necessary for this reactivation were essentially identical with those reported for the reactivation of isolated flagella or whole sperm. ATPase activity of the isolated axostyle was comparable to the values reported for ciliary or flagellar axonemes. The axostyle was reasonably specific for ATP. Most of the proteins of the isolated axostyle comigrated with proteins of the ciliary axoneme on sodium dodecyl sulfate (SDS) polyacrylamide gels (i e. equivalent molecular weights). These included the following: the higher molecular weight component of dynein, tubulin, linkage protein (nexin), and various secondary proteins. Evidence for dynein in the axostyle is presented and a model proposed to explain how repeated propagated waves can be generated.

Efficacy and compatibility with mass spectrometry of methods for elution of proteins from sodium dodecyl sulfate–polyacrylamide gels and polyvinyldifluoride membranes

2004 ◽  
Vol 330 (1) ◽  
pp. 87-97 ◽  
Author(s):  
Charlotte Sværke Jørgensen ◽  
Mitchell Jagd ◽  
Birgitte Kjær Sørensen ◽  
Jim McGuire ◽  
Vibeke Barkholt ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gels ◽  
Dodecyl Sulfate

scholarly journals Transformation-deficient mutants of Bacillus subtilis impaired in competence-specific nuclease activities

1982 ◽  
Vol 152 (1) ◽  
pp. 166-174
Author(s):  
J A Mulder ◽  
G Venema
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Magnesium Ions ◽  
Polyacrylamide Gels ◽  
Wild Type ◽  
Molecular Weights ◽  
Defective Mutant ◽  
Mutant Strains

A comparison of the nucleolytic activities in competent and physiologically low-competent wild-type cultures of Bacillus subtilis in DNA-containing sodium dodecyl sulfate-polyacrylamide gels revealed the existence of three competence-associated nuclease activities with apparent molecular weights of 13,000, 15,000, and 26,000. The three activities, which were dependent on manganese or magnesium ions, were specifically present in the competent fraction of a competent culture. The competence-associated nucleolytic activities of eight transformation-defective mutant strains were assayed, resulting in the following three classes of mutants: (i) four strains which, according to this assay, were not impaired in any of the nucleolytic activities mentioned above; (ii) one strain which was strongly impaired in the 13,000- and 26,000-molecular-weight activities, but showed a considerable level of the 15,000-molecular-weight activity; and (iii) three strains which were severely impaired in all three activities. The results indicated that the 26,000-molecular-weight activity was a dimer of the 13,000-molecular-weight activity and that this nuclease was involved in the entry of DNA.

Detection of N-glycans on small amounts of glycoproteins in tissue samples and sodium dodecyl sulfate–polyacrylamide gels

2012 ◽  
Vol 423 (2) ◽  
pp. 253-260 ◽  
Author(s):  
Takeshi Yoshimura ◽  
Gen Yamada ◽  
Mai Narumi ◽  
Takako Koike ◽  
Akihiro Ishii ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gels ◽  
Tissue Samples ◽  
Dodecyl Sulfate
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