Mercury, Chloro-

The white precipitate which forms is filtered and dried at 80°C, yielding 45 g of chloro-mercuri acid (= 89% of the theory), MP 106° to 109°C (decomp.). This compound is finally obtained in analytically pure form and with a constant melting point by two recrystallizations from acetone-water giving a MP of 131° to 132°C with decomposition. 

A new route, from 1-thio-D-aldohexofuranosides, was developed by Wolfrom and coworkers ethyl 1-thio-a-D-glucofuranoside was converted by chlorine into the chloride,101 arid this was condensed with the chloro-mercuri derivative of a 2,6-diacetamidopurine to give, on partial deacetylation, a 2-acetamido-9- f-D-glucofuranosyladenine.70 D-Galactofuranosyl analogs were also prepared. 

The following compounds 1 are prepared in a similar manner to the corresponding thiophenes, fusion of sulphur or selenium with acetophenone anil giving rise respectively to 2 4-diphenylthiophene and 2 4-diphenylsdencpkene. The melting-points of these compounds and their derivatives are as follows 2 4-diphenylthiophene, M.pt. 122-5° C., 2 4-diphenylselenophene, M.pt. 112-3° C., 5-chloro-mercuri-2 4-diphenylthiophene, M.pt. 223° C., o-chloromercuri-2 4-diphenylselenophene, M.pt. 224° C. 

Chemical modification of soybean agglutinin by acetylation of its amino groups resulted in little loss of agglutinating activity, whereas the protein was quite sensitive to modification of its tyrosyl residues.547 Failure of the protein to react with 2-iodoacetamide or p-(chloro-mercuri)benzoate in 6 M urea confirmed that it was devoid of sulfhydryl groups. A metalloprotein containing151 Ca2+ and Mn2+, the soybean lectin is inactivated by Al3+, Fe3+, and Pb2+, whereas Mn2+, Ba2+, Mg2+, Ag+, Li+, and K+ are without effect.532... 

SYNS CHLORID FENYLRTUTNATY (CZECH) (CHLOROMERCURI)BENZENE FENYLMERCURI-CHLORID (CZECH) MERCURIPHENYL CHLORIDE MERFAZIN iMERSOUTE 2 PHENLX CHLORO-MERCURY PHENYLMERCURY CHLORIDE PHENYLQUECKSILBERCHLORID (GERMAN) PMC STOPSPOT... 

The effects of temperature on the distribution of non-electrolytes between erythrocytes and the surrounding medium in vitro has been investigated with H NMR. The results indicated that between 4° and 37° the rate of uptake by erythrocytes was a function of temperature. The inhibition of water-permeability by diffusion (P ) through the erythrocyte membrane has been investigated using NMR. Maximal inhibition of 50% of Pd was achieved by 2 mM -chloromercuri benzoate in 20 min. The maximal effect of />-chloro-mercuri benzoate was reduced by the presence of lipophilic solutes. However, lipophilic solutes alone caused a faster inhibition of Pd, though this was less efficient than that from p-chloromercuri benzoate. A method has been developed to observe early phosphate penetration into erythrocytes. When the main extracellular cation was Na, 100 mM extracellular Pi penetrated the cells within one hour. When the main extracellular cation was the apparent penetration rate of Pi was reduced by 25%. The influx of Pi into erythrocytes was not accompanied by a change in pHj. ... 

Fig. 27 (79). Reduction of oxidized cytochrome c by Og- produced during the enzy-mic-catalysed oxidation of xanthine. in the presence of catalase (16 nM), erythrocuprein omitted after addition of erythrocuprein (25 nM) and catalase (16 nM) without either erythrocuprein or catalase in the presence of erythrocuprein (25 nM), catalase omitted in the presence of both catalase (16 nM) and p-chloro-mercuri-benzoic acid (400 /iM). The assay was performed at 25 °C in a volume of 0.76 ml. The concentration of the different components dissolved in 50 mM phosphate buffer, pH 7.8 was Xanthine 0.33 mM cytochrome cox, 27 / M EDTA, 0.1 mM xanthine oxidase, 0.21 fiM. The reduction of cytochrome c was recorded in a Unicam SP 1800 spectrophotometer at 550 nm...

Another 2-amino-2-deoxynucleoside, 9-(2-acetamido-2-deoxy-j3-D-ribosyl)-Al ,Al -dimethyladenine (7i),2, 20 s prepared by the reaction of chloro-mercuri-6-chloropurine with the appropriate glycosyl chloride, followed by deblocking with dimethylamine this, again, resulted in concomitant replacement of the C-6-chlorine atom. 

Nebularine has long been known as a metabolite of Clitocybe nebularis (383), revealing tuberculostatic and antimitotic activity (383-385). Few syntheses of this compound having a 9-(D-ribosyl)purine structure have been reported, namely, the Brown (386) approach, starting from a chloro-mercuri-6-purine and 2,3,5-tri-O-acetyl-D-ribofuranosyl chloride, the Fox (387) procedure, based on the transformation of inosine to nebularine via a desulfurization by Raney nickel of the thioinosine intermediate, and the Iwamura-Hashizume (384,388) method, in which nebularine and its N-7 isomer were synthesized simultaneously by the fusion of purine and tetra-O-acetyl-D-ribofuranose using bis(p-nitrophenyl)hydrogen phosphate as the catalyst. 

Indirect chromophore modification was done by titration of trimeric phycocyanin (oB) with PCMS (para-chloro-mercury-benzenesulfonate) in a 1.1-1.2 fold excess (12). 

The exact mechanism of action of the -amino levulinic acid synthetase is not clear. It involves the activation of glycine by pyridoxal phosphate in a Schiff base formation on the enzyme. A proton is lost in the process, and a stable carbanion is formed. In the presence of succinyl CoA, the activated glycine is transferred to succinate, but it is not clear whether the decarboxylation occurs while the succinate and glycine are still attached to the enzyme or later. The activity of the -amino levulinic acid synthetase is inhibited by L-penicillamine, thiosolidine, and L-cysteine. The compounds presumably react with pyridoxal phosphate forming a thiazolidine ring. The enzyme molecule is itself inhibited by the addition of para-chloro-mercuri-benzoic acid. Insofar as succinate is a precursor of 5-amino levulinic acid, the pathway for succinyl CoA synthesis acquires particular significance (refer to the first part of this book). In the reticulocyte, the tricar-... 

Thiols at a concentration of 10 to 40 mM also act as antagonists to the action of neuropeptides on rat uterus, but not to their pressor effect Such a difference could be due to a difference in the receptors. Thioglycollate (10 mM) and cysteine (10 mM) inhibit the permeability response of the toad bladder to oxytocin or vasopressin. Gluthathione has a similar effect These actions of the peptides are also inhibited after incubation of the tissues in the presence of either N-ethyl- or N-phenylaleimide which form covalent bonds with sulphydryl groups or complex mercury mercaptides (p-hydroxy-mercury-benzoate, p-chloro-mercury-benzoate). These results show that the receptor presents in its constitution some functional sulphydryl groups. 

---