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PubMed1966

Acrylamide-gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins.

A mechanical fractionator was developed to produce electrophorograms by extrusion of polyacrylamide gels through a narrow orifice in a continuous, sequential stream. The system permits separation of uniform fractions free of zone distortion. An electrophorogram of radioactive type-2 adenovirus proteins so fractionated gave a pattern in excellent agreement with the pattern obtained by laborious manual sectioning and in agreement with the pattern obtained on a replicate gel stained with Coomassie brilliant blue R250. The adenovirus particle yielded about ten resolvable protein components in unequal amounts. Like picornaviruses, these icosahedral animal viruses have multiple protein components in the viral coat.

Adenoviridae↗
PubMed1978

Acrylamide gel electrophoresis of proteins of Neisseria gonorrhoeae as an epidemiological tool.

The electrophoresis patterns of gonococcal cell proteins were assessed as an aid to gonococcal epidemiology. Lyophilized gonococci were extracted in heated lauryl sulfate with 2-mercaptoethanol. The solubilized gonococcal cell proteins were subjected to alkaline sodium dodecyl sulfate gel electrophoresis, and the resulting patterns were scanned with a spectrophotometer. The electrophoresis patterns were judged to be alike by superimposition of the gel scans. Gonococci thus compared were also auxotyped and tested for sensitivity to penicillin, ampicillin, tetracycline, and spectinomycin. The electrophoresis patterns were reproducible and not affected by serial subculture of the isolates. Patterns from nongonococcal Neisseria species did not resemble those of gonococci. To test the utility of the electrophoresis patterns, duplicate isolates were made from 12 cultures of Neisseria gonorrhoeae. After randomization and blind coding of the 24 isolates, all were successfully matched by their electrophoresis patterns. Cervical-rectal paired isolates from 45 patients were studied by means of their electrophoresis patterns, auxotypes, and results of antibiotic sensitivity tests. Results indicated that the electrophoresis patterns are useful in characterizing paired isolates of gonococci.

Anti-Bacterial Agents↗
PubMed1976

Outer membrane of Escherichia coli K-12: differentiation of proteins 3A and 3B on acrylamide gels and further characterization of con (tolG) mutants.

Two classes of mutants, con and tolG, that appeared to be very similar in a number of respects have been shown to be identical and cotransducible with pyrD. By diethylaminoethyl-cellulose chromatography of the outer membranes, we have shown that the mutants are missing only protein 3A and retain protein 3B. Using con mutants, we were thus able to identify protein 3B on the pH 7.2 gel system of Maizel where it runs separately from protein 3A if unheated samples are used. tolG mutants were shown to be identical to con mutants in being conjugation defective with most F-like plasmid donors but not with I-like plasmid donors, and in their resistance pattern to bacteriophages and colicins. During the course of this study, it was observed that the bacteriocin produced by Serratia marcescenc JF246 was identical in its activity spectrum to colicin L-398 and is now considered to be a colicin of type L.

Anti-Bacterial Agents↗
PubMed1976

An acrylamide gel recombination assay for glycoprotein hormone subunits.

A specific and sensitive assay for recombination of the subunits of hCG and other glycoprotein hormones (LH, FSH, and TSH) is presented. The assay depends on the ability of sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) to separate clearly the subunits from native hormone. Iodinated subunit is incubated with its identical unlabeled subunit and complementary subunit. Quantitative displacement of the radioactivity to the native hormone position as followed by gel slicing is used as a direct index of recombination. The assay is reproducible, sensitive to less than one picomole of hormone formed, and offers a simple means of evaluating recombination of glycoprotein chains as distinct from biological activity.

Chorionic Gonadotropin↗