@article {91, title = {Acid-base balance in amphibian gastric mucosa.}, journal = {Am J Physiol}, volume = {229}, year = {1975}, month = {1975 Sep}, pages = {721-30}, abstract = {

It has been established that H+ secretion can be maintained in frog stomach in the absence of exogenous CO2 by using a nutrient bathing fluid containing 25 mM H2PO4 (pH approximately equal to 4.5) or by lowering the pH of a nonbuffered nutrient solution to about 3.0-3.6. Exogenous CO2 in the presence of these nutrient solutions uniformly caused a marked decrease in H+ secretion, PD, adn short-circuit current (Isc) and an increase in transmucosal resistance (R). Elevation of nutrient [k+] to 83 mM reduced R significantly but transiently without change in H+ when nutrient pH less than 5.0, whereas R returned to base line and H+ increased when nutrient pH greater than 5.0. Acidification of the nutrient medium in the presence of exogenous CO2 results in inhibition of the secretory pump, probably by decreasing intracellular pH, and also interferes with conductance at the nutrient membrane. Removal of exogenous CO2 from standard bicarbonate nutrient solution reduced by 50\% the H+, PD, and Isc without change in R; K+-free nutrient solutions reverse these changes in Isc and PD but not in H+. The dropping PD and rising R induced by K+-free nutrient solutions in 5\% CO2 - 95\% O2 are returned toward normal by 100\% O2. Our findings support an important role for exogenous CO2 in maintaining normal acid-base balance in frog mucosa by acting as an acidifying agent.

}, keywords = {Acid-Base Equilibrium, Animals, Anura, Bicarbonates, Carbon Dioxide, Electrophysiology, Gastric Mucosa, Hydrogen-Ion Concentration, Phosphates, Potassium, Rana catesbeiana, Solutions}, issn = {0002-9513}, author = {Silen, W and Machen, T E and Forte, J G} } @article {92, title = {Recombination of ciliary dynein of Tetrahymena with the outer fibers.}, journal = {J Biochem}, volume = {78}, year = {1975}, month = {1975 Jul}, pages = {41-9}, abstract = {

Recombination of ciliary dyneins of Tetrahymena pyriformis with the outer fibers was investigated using turbidimetry, co-sedimentation analysis and electron microscopy. As reported by Gibbons, 30S dynein could recombine with the outer fibers, while 14S dynein did to so a lesser extent. At acidic pH, however, most of the 14S dynein was also rebound to the outer fibers. When an excess of crude dynein fraction was added to the outer fiber fraction at pH 8.2, electron microscopic observations showed that the outer doublet microtubules were decorated not only with arms but also with other electron-dense materials. On the other hand, when crude dynein fraction was mixed with the outer fibers in an appropriate quantity, only arms were reconstituted at the regular positions of A-subfibers. ATP had an inhibitory effect on the recombination of dynein with the outer fibers.

}, keywords = {Adenosine Triphosphatases, Adenosine Triphosphate, Cilia, Flagella, Hydrogen-Ion Concentration, Magnesium, Microtubules, Nephelometry and Turbidimetry, Tetrahymena}, issn = {0021-924X}, author = {Shimizu, T} } @article {97, title = {Studies on variant glucose-6-phosphate dehydrogenases: G6PD Fort Worth.}, journal = {Biochem Med}, volume = {13}, year = {1975}, month = {1975 Jul}, pages = {264-75}, keywords = {Adult, Drug Stability, Erythrocytes, Female, Genetic Variation, Glucosephosphate Dehydrogenase, Humans, Hydrogen-Ion Concentration, Kinetics, Male, Temperature, Texas}, issn = {0006-2944}, author = {Mills, G C and Alperin, J B and Trimmer, K B} } @article {99, title = {Malathion A and B esterases of mouse liver-I.}, journal = {Biochem Pharmacol}, volume = {24}, year = {1975}, month = {1975 Sep 15}, pages = {1713-7}, keywords = {Animals, Drug Stability, Esterases, Female, Hydrogen-Ion Concentration, Liver, Malathion, Male, Metals, Mice, Sex Factors, Sulfhydryl Compounds}, issn = {0006-2952}, author = {Bhagwat, V M and Ramachandran, B V} } @article {101, title = {Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase.}, journal = {Biochem Pharmacol}, volume = {24}, year = {1975}, month = {1975 Aug 15}, pages = {1517-21}, keywords = {Amidohydrolases, Animals, Esterases, Hydrogen-Ion Concentration, In Vitro Techniques, Isocarboxazid, Kinetics, Male, Metals, Microsomes, Liver, Phospholipids, Procaine, Proteins, Rats, Subcellular Fractions, Temperature}, issn = {0006-2952}, author = {Moroi, K and Sato, T} } @article {102, title = {Formate assay in body fluids: application in methanol poisoning.}, journal = {Biochem Med}, volume = {13}, year = {1975}, month = {1975 Jun}, pages = {117-26}, keywords = {Aldehyde Oxidoreductases, Animals, Body Fluids, Carbon Dioxide, Formates, Haplorhini, Humans, Hydrogen-Ion Concentration, Kinetics, Methanol, Methods, Pseudomonas}, issn = {0006-2944}, author = {Makar, A B and McMartin, K E and Palese, M and Tephly, T R} } @article {103, title = {Peptide-binding macromolecules in the blood of seriously ill or mentally retarded patients.}, journal = {J Lab Clin Med}, volume = {87}, year = {1976}, month = {1976 Feb}, pages = {299-319}, abstract = {

This report describes macromolecules that bind (des-aspartic acid1)-angiotensin II, the des aspartic acid1 derivative of angiotensin I, and several biologically active and inactive analogues of these polypeptides. The macromolecules were found in the plasma of approximately 2 per cent of ambulatory adults and hospitalized children and 32 per cent of the patients at two institutions for the mentally retarded. The binding properties of these macromolecules were studied by incubating with peptides labeled with 125iodine, and separating bound from free labeled peptide using small gel filtration columns. The peptide-binding macromolecules from several patients were compared. They showed very similar specificity for a group of arginyl peptides of the des-aspartyl1-angiotensin sequence. The plasma binders differed from one another in their optimum pH and their mobility in electrophoretic fields. Those with more acid pH optima displayed more rapid electrophoretic mobility. The binders fell into two classes based on apparent molecular weight, approximately 140,000 and 250,000. Those with the higher apparent molecular weight contained a large proportion of binder that could be precipitated with antiserum to human IgA. Kinetic measurements showed that the plasma binders were somewhat heterogeneous with respect to affinity for (des-asp1)-angiotensin, with apparent association constants ranging from 10(7) to 10(8) M-1. Binding activity was labile to heat, and to treatment with pepsin or trypsin. It was inhibited by calcium, protamine, streptomycin, and some other cationic compounds. The plasma peptide binder differed in specificity and molecular weight from soluble angiotensin-binding molecules extracted from tissues, and from properties expected of a receptor for angiotensin. These macromolecules may be useful reagents for measuring (des-asp1)-angiotensins. Their presence in plasma samples may interfere with angiotensin assays in some circumstances.

}, keywords = {Angiotensin II, Chromatography, Gel, Electrophoresis, Starch Gel, Humans, Hydrogen-Ion Concentration, Intellectual Disability, Kidney Failure, Chronic, Kinetics, Macromolecular Substances, Neoplasms, Osmolar Concentration, Peptides, Protein Binding, Saralasin}, issn = {0022-2143}, author = {Goodfriend, T L and Sindel, M and Fyhrquist, F and Hong, R and Azen, E and Stewart, J M} } @article {104, title = {The reaction of choline and 3,3-dimethyl-1-butanol with the acetylenzyme from acetylcholinesterase.}, journal = {J Neurochem}, volume = {25}, year = {1975}, month = {1975 Dec}, pages = {783-7}, keywords = {Acetylcholinesterase, Binding Sites, Choline, Hexanols, Hydrogen-Ion Concentration, Kinetics, Mathematics, Osmolar Concentration, Protein Binding, Sodium Chloride}, issn = {0022-3042}, author = {Dawson, R M} }