Ramakrishna S, Adiga PR. Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properites. Eur J Biochem. 1975;59 (2) :377-86.Abstract
Arginine decarboxylase which makes its appearance in Lathyrus sativus seedlings after 24 h of seed germination reaches its highest level around 5-7 days, the cotyledons containing about 60% of the total activity in the seedlings at day 5. The cytosol enzyme was purified 977-fold from whole seedlings by steps involving manganese chloride treatment, ammonium sulphate and acetone fractionations, positive adsorption on alumina C-gamma gel, DEAE-Sephadex chromatography followed by preparative disc gel electrophoresis. The enzyme was shown to be homogeneous by electrophoretic and immunological criteria, had a molecular weight of 220,000 and appears to be a hexamer with identical subunits. The optimal pH and temperature for the enzyme activity were 8.5 and 45 degrees C respectively. The enzyme follows typical Michaelis-Menten kinetics with a Km value of 1.73 mM for arginine. Though Mn2+ at lower concentrations stimulated the enzyme activity, there was no dependence of the enzyme on any metal for the activity. The arginine decarboxylase of L. sativus is a sulfhydryl enzyme. The data on co-factor requirement, inhibition by carbonyl reagents, reducing agents and pyridoxal phosphate inhibitors, and a partial reversal by pyridoxal phosphate of inhibition by pyridoxal-HCl suggests that pyridoxal 5'-phosphate is involved as a co-factor for the enzyme. The enzyme activity was inhibited competitively by various amines including the product agmatine. Highest inhibition was obtained with spermine and arcain. The substrate analogue, L-canavanine, homologue L-homoarginine and other basic amino acids like L-lysine and L-ornithine inhibited the enzyme activity competitively, homoarginine being the most effective in this respect.
Makar AB, McMartin KE, Palese M, Tephly TR. Formate assay in body fluids: application in methanol poisoning. Biochem Med. 1975;13 (2) :117-26.
Shibaeva AN. [The organization of health education meetings, verbal reports, carnivals, reader's conferences]. Feldsher Akush. 1975;40 (9) :31-4.
Tucker GT. Plasma binding and disposition of local anesthetics. Int Anesthesiol Clin. 1975;13 (4) :33-59.
Haefely W, Kulcsár A, Möhler H. Possible involvement of GABA in the central actions of benzodiazepines. Psychopharmacol Bull. 1975;11 (4) :58-9.
Tominaga Y, Tsujisaka Y. Purification and some enzymatic properties of the chitosanase from Bacillus R-4 which lyses Rhizopus cell walls. Biochim Biophys Acta. 1975;410 (1) :145-55.Abstract
A strain of Bacillus sp (Bacillus R-4) produces a protease and a carbohydrolase both of which have the ability to lyse Rhizopus cell walls. Of the enzymes, the carbohydrolase has been purified to an ultracentrifugally and electrophoretically homogeneous state, and identified as a chitosanase. The enzyme was active on glycol chitosan as well as chitosan. Molecular weight of the purified enzyme was estimated as 31 000 and isoelectric point as pH 8.30. The enzyme was most active at pH 5.6 and at 40 degrees C with either Rhizopus cell wall or glycol chitosan as substrate, and was stable over a range of pH 4.5 to 7.5 at 40 degrees C for 3 h. The activity was lost by sulfhydryl reagents and restored by either reduced glutathione of L-cysteine. An abrupt decrease in viscosity of the reaction mixture suggested an endowise cleavage of chitosan by this enzyme.
Vyhnánek L. [Fused vertebrae in archeological skeletal material]. Anthropol Anz. 1972;33 (3) :258-66.
[Arkadiĭ Nikolaevich Tsellarius]. Klin Khir. 1970;6 :89.
Mackender RO, Leech RM. Isolation of chloroplast envelope membranes. Nature. 1970;228 (5278) :1347-9.
Petritchev M, Lazarov V. [Research on chlorophos-32 elimination from rabbit and ewe organisms]. Bull Acad Vet Fr. 1969;42 (9) :889-95.
Tarnecki R, Konorski J. Instrumental conditioning of thalamogenic movements and its dependence on the cerebral cortex. Acta Biol Exp (Warsz). 1969;29 (1) :17-28.
Conio G, Patrone E, Tealdi A, Bianchi E. Conformational properties of poly-L-ornithine in aqueous solution. Ric Sci. 1969;39 (1) :61-7.
Janis R, Hamerman D. Articular cartilage changes in early arthritis. Bull Hosp Joint Dis. 1969;30 (2) :136-52.
Battegay R. [Professor Dr. med. Heinrich Meng. On his 80th birthday]. Prax Kinderpsychol Kinderpsychiatr. 1968;17 (2) :33-4.
Postel EH, Goodgal SH. Uptake of "single-stranded" DNA in Hemophilus influenzae and its ability to transform. J Mol Biol. 1966;16 (2) :317-27.
Zamfirescu NR. [Circulatory homeostasis in physical exertion]. Stud Cercet Fiziol. 1966;11 (2) :97-119.