Hybridoma Screening by Antigen Capture: Immunoprecipitation

2022 ◽  
Vol 2022 (1) ◽  
pp. pdb.prot103143
Author(s):  
Edward A. Greenfield

Immunoprecipitation is rarely used for screening hybridoma fusions because the assays are tedious and time-consuming. However, it can be useful when working with complex antigens because the precipitated antigen is normally detected after sodium dodecyl sulfate (SDS)–polyacrylamide electrophoresis and thus it is simple to discriminate between true and false positives. Furthermore, the assay provides information regarding the molecular weight of the antigen.

1973 ◽  
Vol 56 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Mark S. Mooseker ◽  
Lewis G. Tilney

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.


1980 ◽  
Vol 58 (1) ◽  
pp. 67-72
Author(s):  
D. J. S. Arora ◽  
L. Vincent ◽  
J. Hill-Schubert

A ribonuclease activity associated with influenza virus has been purified to homogeneity. This preparation is free of DNAase, phosphodiesterase, and phosphatase activities. The purified enzyme has a pH optima of 7.0 at 37 °C, and moves as a single band on sodium dodecyl sulfate – polyacrylamide gel with an estimated molecular weight of 84 000.


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