Publications

1975
UN Wiesmann, S DiDonato, and NN Herschkowitz. 1975. “Effect of chloroquine on cultured fibroblasts: release of lysosomal hydrolases and inhibition of their uptake.” Biochem Biophys Res Commun, 66, 4, Pp. 1338-43.
N Worathumrong and AJ Grimes. 1975. “The effect of o-salicylate upon pentose phosphate pathway activity in normal and G6PD-deficient red cells.” Br J Haematol, 30, 2, Pp. 225-31.Abstract
The effect of the major metabolite of aspirin, namely salicylic acid, upon the pentose phosphate pathway (PPP) of normal and G6PD-deficient red cells has been studied. Salicylic acid was shown to inhibit this pathway in proportion to the amount present. At any concentration of this substance there was greater inhibition of the PPP in G6PD-deficient than in normal red cells.
B Renaud, M Buda, BD Lewis, and JF Pujol. 1975. “Effects of 5,6-dihydroxytryptamine on tyrosine-hydroxylase activity in central catecholaminergic neurons of the rat.” Biochem Pharmacol, 24, 18, Pp. 1739-42.
LM Mal'steva, PN Liubchenko, ZI Boiarchuk, and Iu M Shternberg. 1975. “[Electrolytes and acid-base balance in the blood of workers exposed to the action of fluorine compounds].” Gig Tr Prof Zabol, 10, Pp. 49-50.
AB Makar, KE McMartin, M Palese, and TR Tephly. 1975. “Formate assay in body fluids: application in methanol poisoning.” Biochem Med, 13, 2, Pp. 117-26.
RJ Lefkowitz. 1975. “Identification of adenylate cyclase-coupled beta-adrenergic receptors with radiolabeled beta-adrenergic antagonists.” Biochem Pharmacol, 24, 18, Pp. 1651-8.
J Haveman and J Lavorel. 1975. “Identification of the 120 mus phase in the decay of delayed fluorescence in spinach chloroplasts and subchloroplast particles as the intrinsic back reaction. The dependence of the level of this phase on the thylakoids internal pH.” Biochim Biophys Acta, 408, 3, Pp. 269-38.Abstract
After a 500 mus laser flash a 120 mus phase in the decay of delayed fluorescence is visible under a variety of circumstances in spinach chloroplasts and subchloroplast particles enriched in Photosystem II prepared by means of digitonin. The level of this phase is high in the case of inhibition of oxygen evolution at the donor side of Photosystem II. Comparison with the results of Babcock and Sauer (1975) Biochim. Bio-phys. Acta 376, 329-344, indicates that their EPR signal IIf which they suppose to be due to Z+, the oxidized first secondary donor of Photosystem II, is well correlated with a large amplitude of our 120 mus phase. We explain our 120 mus phase by the intrinsic back reaction of the excited reaction center in the presence of Z+, as predicted by Van Gorkom and Donze (1973) Photochem. Photobiol. 17, 333-342. The redox state of Z+ is dependent on the internal pH of the thylakoids. The results on the effect of pH in the mus region are compared with those obtained in the ms region.
N Akamatsu, H Nakajima, M Ono, and Y Miura. 1975. “Increase in acetyl CoA synthetase activity after phenobarbital treatment.” Biochem Pharmacol, 24, 18, Pp. 1725-7.
VM Roemer, K Harms, K Hammacher, and M Hinselmann. 1975. “[Indications for cesarean section: indication and status of the newborn infant after surgery].” Arch Gynakol, 219, 1-4, Pp. 482-4.
F Dubouloz, D Moisan, B Signouret, and J Faizende. 1975. “[Infectious problems in reoperations in abdominal surgery. Apropos of 104 operations].” Ann Anesthesiol Fr, 16, 4, Pp. 284-8.Abstract
Analysis of the problems with infection in a series of 104 reinterventions, enables one to accentuate the importance of infestation from intraperitoneal foci (70 p. 100 of the cases). Extra-peritoneal entry pathways are difficult to prove. Septicemia is found in one out of every three cases. In certain cases, preventive treatment of the extra-peritoneal entry pathways must be opposed to the effectiveness of the surgical act in the eradication of septic foci.
DH Pocock and DJ Garwes. 1975. “The influence of pH on the growth and stability of transmissible gastroenteritis virus in vitro.” Arch Virol, 49, 2-3, Pp. 239-47.Abstract
The influence of pH on the growth of transmissible gastroenteritis virus (TGEV) in adult pig thyroid cell culture, and on the stability of the virus was studied. At pH 7.2 and 100 fold higher than those at pH 8.0. The adsorption, penetration and uncoating steps of the viral replicative cycle were shown to be unaffected by pH variation. Synthesis of TGEV RNA during the first 12 hours post infection was found to be unaffected by pH variation between the range 6.5-8.0. After 12 hours breakdown of this RNA appeared to occur in cultures held at pH 7.2 and 8.0 but not at pH 6.5. When incubated at 37 degrees C for 24 hours the virus infectivity was found to be least affected by pH 6.5 but when kept at 4 degrees C for the same length of time, the virus infectivity remained constant between pH 5.0 and pH 8.0.
AJ Turner and PE Hick. 1975. “Inhibition of aldehyde reductase by acidic metabolites of the biogenic amines.” Biochem Pharmacol, 24, 18, Pp. 1731-3.
MM Ris, RA Deitrich, and JP Von Wartburg. 1975. “Inhibition of aldehyde reductase isoenzymes in human and rat brain.” Biochem Pharmacol, 24, 20, Pp. 1865-9.
DJ Goss, LJ Parkhurst, and H Görisch. 1975. “Kinetic light scattering studies on the dissociation of hemoglobin from Lumbricus terrestris.” Biochemistry, 14, 25, Pp. 5461-4.Abstract
The kinetics of the pH-induced dissociation of the 3 X 10(6) mol wt hemoglobin from Lumbricus terrestris (the earthworm) have been studied in a light-scattering stopped-flow apparatus. The ligand dependent dissociation data were fit well by a simple sequential model. The data for CO and oxyhemoglobin are consistent with Hb12 leads to 2Hb6 leads to 12Hb. Methemoglobin at pH 7 appears to be hexameric and the dissociation is consistent with the model: Hb6 leads to 6Hb. In a sequential decay scheme for which light-scattering changes are monitored, the relative amounts of rapid and slow phase are determined by the rate constants as well as the molecular weights of intermediate species. Assignment of the hexameric intermediate is supported by an investigation of the sensitivity of the theoretical kinetic curves to the molecular weights of the intermediates. This assignment is further supported by the following: (1) the same model will fit the data for oxy- and CO-hemoglobin at all three temperatures (a 24-29-fold variation in rate constants), (2) evidence from electron microscopy shows hexameric forms, and (3) methemoglobin is apparently stable as a hexamer at pH 7. When CO replaces O2 as the ligand, the dissociation rate increases by a factor of four. The met is about 20 times faster than the initial oxyhemoglobin dissociation rate, but perhaps more relevant for comparing dissociation of the hexamer, the met rate was respectively 100 times and 500 times faster than that for the assumed hexameric forms of CO- and oxy-hemoglobin. The activation energies for the dodecamer to hexamer dissociation and for the dissociation of the hexamer to smaller forms were about 30 kcal/mol for oxy-, CO-, and methemoglobin.
HJ Van Gorkom, MP Pulles, and JS Wessels. 1975. “Light-induced changes of absorbance and electron spin resonance in small photosystem II particles.” Biochim Biophys Acta, 408, 3, Pp. 331-9.Abstract
Photosystem II reaction center components have been studied in small system II particles prepared with digitonin. Upon illumination the reduction of the primary acceptor was indicated by absorbance changes due to the reduction of a plastoquinone to the semiquinone anion and by a small blue shifts of absorption bands near 545 nm (C550) and 685 nm. The semiquinone to chlorophyll ratio was between 1/20 and 1/70 in various preparations. The terminal electron donor in this reaction did not cause large absorbance changes but its oxidized form was revealed by a hitherto unknown electron spin resonance (ESR) signal, which had some properties of the well-known signal II but a linewidth and g-value much nearer to those of signal I. Upon darkening absorbance and ESR changes decayed together in a cyclic or back reaction which was stimulated by 3-(3,4 dichlorophenyl)-1,1-dimethylurea. The donor could be oxidized by ferricyanide in the dark. Illumination in the presence of ferricyanide induced absorbance and ESR changes, rapidly reversed upon darkening, which may be ascribed to the oxidation of a chlorophyll a dimer, possibly the primary electron donor of photosystem II. In addition an ESR signal with 15 to 20 gauss linewidth and a slower dark decay was observed, which may have been caused by a secondary donor.
VM Bhagwat and BV Ramachandran. 1975. “Malathion A and B esterases of mouse liver-I.” Biochem Pharmacol, 24, 18, Pp. 1713-7.
T Randerson, James and TA Slotkin. 1975. “Maturation of the adrenal medulla--IV. Effects of morphine.” Biochem Pharmacol, 24, 16, Pp. 1469-74.
RJ Smith and RG Bryant. 1975. “Metal substitutions incarbonic anhydrase: a halide ion probe study.” Biochem Biophys Res Commun, 66, 4, Pp. 1281-6.
HF Gilbert and MH O'Leary. 1975. “Modification of arginine and lysine in proteins with 2,4-pentanedione.” Biochemistry, 14, 23, Pp. 5194-9.Abstract
Primary amines react with 2,4-pentanedione at pH 6-9 to form enamines, N-alkyl-4-amino-3-penten-2-ones. The latter compounds readily regenerate the primary amine at low pH or on treatment with hydroxylamine. Guanidine and substituted guanidines react with 2,4-pentanedione to form N-substituted 2-amino-4,6-dimethylpyrimidines at a rate which is lower by at least a factor of 20 than the rate of reaction of 2,4-pentanedione with primary amines. Selective modification of lysine and arginine side chains in proteins can readily be achieved with 2,4-pentanedione. Modification of lysine is favored by reaction at pH 7 or for short reaction times at pH 9. Selective modification of arginine is achieved by reaction with 2,4-pentanedione for long times at pH 9, followed by treatment of the protein with hydroxylamine. The extent of modification of lysine and arginine side chains can readily be measured spectrophotometrically. Modification of lysozyme with 2,4-pentanedione at pH 7 results in modification of 3.8 lysine residues and less than 0.4 arginine residue in 24 hr. Modification of lysozyme with 2,4-pentanedione at pH 9 results in modification of 4 lysine residues and 4.5 arginine residues in 100 hr. Treatment of this modified protein with hydroxylamine regenerated the modified lysine residues but caused no change in the modified arginine residues. One arginine residue seems to be essential for the catalytic activity of the enzyme.
M Anai, T Mihara, M Yamanaka, T Shibata, and Y Takagi. 1975. “A nucleoside triphosphate-dependent deoxyribonuclease from Bacillus laterosporus. Purification and characterization of the enzyme.” J Biochem, 78, 1, Pp. 105-14.Abstract
A deoxyribonuclease, which requires nucleoside triphosphate for reaction, has been purified about 150-fold from extracts of Bacillus laterosporus. Potassium phosphate and ethylene glycol stabilize the purified enzyme. The enzyme degrades double-stranded DNA about 100 times faster than heat-denatured DNA in the presence of nucleoside triphosphate. Double-stranded DNA is not degraded to any measurable extent in the absence of ATP, but the enzyme exhibits activity toward denatured DNA in the absence of nucleoside triphosphate, and this activity seems to be an intrinsic property of this enzyme protein. The optimum pH is 8.5 and the maximum activity is obtained in the copresence of Mg2+ (8.0 X 10(-3)M) and Mn2+ (7.0 X 10(-5)M). ATP and dATP are most effective and nucleoside di- or monophosphates are ineffective. ATP is converted to ADP and inorganic phosphate during the reaction and the ratio of the amount of ATP cleaved to that of hydrolyzed phosphodiester bonds of DNA is about 3:1. An inhibitor of the enzyme was observed in bacterial extracts prepared by sonic disruption; the inhibitory substance is produced in the bacteria in the later stages of cell growth. Preliminary results show that the inhibitor emerged near the void volume of a Sephadex G-200 column, and was relatively heat-stable, RNase-resistant, and DNase-sensitive.

Pages