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Biomedical subjects

M Blecher

Publications and source records attributed to M Blecher.

At least 37 records · Page 2Linked to original sources
PubMed1987

A patent law primer for clinical chemists and other scientists.

Patenting and commercialization by academic scientists, despite potential drawbacks, are on balance highly desirable if technology is to be transferred from the laboratory to the public use, and if the scientist and his institution are to be encouraged to participate in this transfer. If that premise is accepted, there is much that academic institutions can do to foster utilization of their biotechnological discoveries. Such institutions should have a patent policy that is known to all and that includes a professional patent administrator and clear administrative procedures for carrying out such policy. Scientists should be trained to recognize and protect their inventions and to appropriately disclose their inventions to their patent officers. Ideally, scientists should know the rudiments of the patent statutes of their own country and should be aware of what constitutes trade secrets. Scientists should be given guidance in working with patent attorneys in the preparation and prosecution of patent applications. Finally, given human nature, institutions should see to it that their scientists are provided with a suitable environment in which to invent, and appropriate incentives to do so.

Chemistry, Clinical↗
PubMed1984

Partial purification of a water-soluble liver protein that regulates adenylate cyclase activity (basal, hormone- and cholera-toxin-activated) and cholera-toxin-catalyzed ADP-ribosylation of the membrane G protein.

We have found in water-soluble extracts of rat liver (and RL-PR-C cloned rat hepatocytes), prepared in the absence of detergent, a factor that markedly enhances basal, isoproterenol and cholera toxin activation of adenylate cyclase of rigorously washed hepatocyte membranes, in the absence of added GTP. The factor, which has characteristics of a protein with an Mr of approx. 35000, has been fractionated from crude cytosol by gel filtration, and then further purified over 50-fold by sequential ion-exchange chromatography. The site of action of the protein appears to be at the level of the guanine nucleotide regulatory (G) protein of the plasma membrane adenylate cyclase complex, as the factor, cooperatively with GTP, also permitted cholera toxin to ADP-ribosylate (from 32P-labeled NAD) two integral membrane proteins that migrated on SDS-polyacrylamide gel electrophoresis gels with the mobilities (Mr approx. 46 000 and 48 000) generally observed for the guanine nucleotide regulator protein subunits. In this system, isoproterenol did not stimulate ADP-ribosylation, in either the presence or absence of the liver protein factor.

Adenosine Diphosphate Ribose↗
PubMed1984

Beta-blocking autoantibodies in pediatric bronchial asthma.

We have used the inhibition of binding of a potent beta antagonist, iodohydroxybenzylpindolol, to canine lung-plasma membrane beta-adrenergic receptors as a test for beta-blocking autoantibodies in the sera of 376 mildly and severely asthmatic children. This binding inhibition assay, coupled with a variant test in which the binding assay was performed on selected sera (binding values below 2 SD from the mean) before and after immunodepletion of the sera (removal of IgG and IgA), permitted the conclusion that about 5% of the juvenile asthmatic population studied produce beta-blocking autoantibodies.

Adrenergic beta-Antagonists↗
PubMed1984

Cortical tubular and glomerular dopamine receptors in the rat kidney.

Dopamine receptors in glomeruli and renal cortical tubules were characterized using radioligand binding and adenylate cyclase studies. The binding of [3H]haloperidol to glomeruli and tubules was rapid, saturable with time and ligand concentration, reversible, of high affinity, and demonstrated stereoselectivity and antagonist and agonist rank potency for binding to dopamine receptors. Analysis of kinetic data and Rosenthal plots in glomeruli revealed a single class of [3H]haloperidol binding sites with an apparent dissociation constant (Kd) of 6 nM and maximum receptor density (Bmax) of 0.42 pmol/mg protein. In tubules, at least two binding sites were noted, one with an apparent Kd of 38 nM and Bmax of 1.90 pmol/mg protein and another with an apparent Kd of 183 nM and Bmax of 3.50 pmol/mg protein. Dopamine and apomorphine increased adenylate cyclase in tubular membranes while no increases were noted in glomeruli. These studies suggest that glomeruli have D2 dopamine receptors, while renal cortical tubules contain the D1 dopamine receptor.

Adenylyl Cyclases↗
PubMed1984

Dopamine receptors in the proximal tubule of the rabbit.

Our laboratory has characterized dopamine receptors in glomeruli and tubular homogenates. Since the heterogeneity of kidney homogenates limits the interpretation of these studies, the [3H]haloperidol binding site and adenylate cyclase sensitivity to dopamine were studied in the isolated proximal convoluted tubule and pars recta of the rabbit kidney. [3H]Haloperidol binding sites were saturable, stereoselective, and of high affinity. The apparent dissociation constant was 31.5 X 10(-9) M (+/- 8.5) and the maximum receptor density was 0.31 X 10(-15) M (+/- 0.08) per millimeter. In pars recta specific binding was 53% of total [3H]-haloperidol binding. Dopamine stimulated adenylate cyclase activity in a dose-related manner, which was inhibited by cis-flupenthixol but not by trans-flupenthixol or (-)-propranolol. Moreover, the stimulatory effect of the dopamine 1 (D1) agonist SKF 82526 on adenylate cyclase activity was blocked by the D1 antagonist SCH 23390. Dopamine receptors in the proximal convoluted tubule appear to be of the D1 subtype since they are linked to stimulation of adenylate cyclase. This is further substantiated by the stereoselectivity for (+)-sulpiride (a D1 antagonist), which had a greater affinity for the [3H]haloperidol binding site than (-)-sulpiride (a D2 antagonist).

Adenylyl Cyclases↗