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Dive into the research topics where John A. Brockman is active.

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Featured researches published by John A. Brockman.


Experimental Biology and Medicine | 1957

Multiple nature of inhibitory factor (factor I) from brain.

John A. Brockman; Sherman L. Burson

Summary Extracts of fresh mammalian brain contained substances which inhibited the “slow” closer and opener systems of the crayfish claw. Glutamic acid was one of the substances. Aspartic acid and γ-aminobutyric acid were also active. Glutamic acid had an inhibitory effect and aspartic acid had a stimulatory effect on the crayfish heart.


Experimental Biology and Medicine | 1953

Heparin-like anticoagulants from Mollusca.

Laurence H. Frommhagen; Marvin J. Fahrenbach; John A. Brockman; E. L. R. Stokstad

Summary Heparin-like polysaccharides with high anticoagulant activity have been isolated from 2 species of clams, Mactra spissula and Artica islandica. These purified polysaccharides, termed mactin-A and mac-tin-B, are related to but not identical with mammalian heparin. They possess a greater in vivo activity and a favorable therapeutic index when compared with heparin preparations of equal in vitro activity.


The Journal of Allergy and Clinical Immunology | 1982

Effects of iodipamide on human C3 and factor B in vitro

Paul J. Durda; Robert J. Pagano; Norman Bauman; John A. Brockman

The effects of iodipamide on C3 and factor B in normal human serum and in purified form have been examined by immunoelectrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Temperature-dependent changes in immunoelectrophoretic profiles have been observed; however, these are not the same as those obtained after treatment of normal human serum (NHS) with cobra venom factor Naja naja. Analyses of iodipamide-treated NHS and purified C3 and factor B by reducing SDS-PAGE indicate that no macromolecular changes have occurred in C3 and factor B that can be ascribed to proteolysis (i.e., activation). The changes observed in C3 and factor B, including loss of hemolytic activity, appear to be due to direct interactions between iodipamide and C3 and factor B. In the case of factor B, iodipamide treatment at 37 degrees C induces aggregation, which is reversible upon reduction with beta-mercaptoethanol.


Journal of Medicinal Chemistry | 1990

Preparation of triazolo[1,5-c]pyrimidines as potential antiasthma agents

Medwid Jb; Rolf Paul; Baker Js; John A. Brockman; Du Mt; William Hallett; Hanifin Jw; Hardy Ra; Tarrant Me; Lawrence Wayne Torley


Journal of Medicinal Chemistry | 1985

Imidazo[1,5-d][1,2,4]triazines as potential antiasthma agents.

Rolf Paul; John A. Brockman; William Hallett; John W. Hanifin; M. Ernestine Tarrant; Lawrence Wayne Torley; Francis M. Callahan; Paul Frank Fabio; Bernard D. Johnson


Archive | 1974

Linear determination of hemolytic complement activity in undiluted serum

Norman Bauman; John A. Brockman


Journal of Nutrition | 1952

Comparative biological activity of leucovorin and pteroylglutamic acid.

Harry P. Broquist; John A. Brockman; Marvin J. Fahrenbach; E. L. R. Stokstad; T. H. Jukes


Archive | 1971

Process for separating proteins from central nervous system tissue and treating experimentally induced demyelinating diseases

John A. Brockman


Archive | 1956

Salts of substituted tetrahydroformyl pteroyl amino acids

John A. Brockman; Roth Barbara


Archive | 1984

5-substituted[1,2,4]triazolo[1,5-c]pyrimidin-2-amines

Rolf Paul; Robert Allis Hardy; John A. Brockman

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