Characterization of products from chloro(diethylenetriamine)platinum(1+) chloride and S-adenosyl-L-homocysteine. Evidence for a pH-dependent migration of the platinum moiety from the sulfur atom to the amine group and vice versa

1990 ◽  
Vol 29 (10) ◽  
pp. 1880-1884 ◽  
Author(s):  
Edwin L. M. Lempers ◽  
Jan Reedijk
Keyword(s):  
2000 ◽  
Vol 88 (2) ◽  
Author(s):  
D. Rößler ◽  
K. Franke ◽  
R. Süß ◽  
E. Becker ◽  
H. Kupsch

A natural moor soil humic acid (HA) was labeled with Tc-99m via reduction of pertechnetate with stannous chloride. The humic acid species obtained were characterized by thin layer chromatography (TLC), gel permeation chromatography (GPC), sequential chromatographic analysis (SCA), paper electrophoresis and micropore filtration. Labeling was found to take place in all ranges of molecular weight. Due to the complex humic acid composition and the formation of hydroxo species the labeling yields strongly depend on the separation conditions, ranging from 42% to 80%. The pH-dependent distribution of mobile and immobile species was determined by SCA for HTcO


2019 ◽  
Vol 116 (3) ◽  
pp. 83a ◽  
Author(s):  
Luis Santiago-Ortiz ◽  
Morgan Hitchner ◽  
Thaddeus Palmer ◽  
Gregory A. Caputo

1981 ◽  
Vol 36 (5-6) ◽  
pp. 400-406 ◽  
Author(s):  
Toshihisa Ohshima ◽  
Gerhart Drews

Abstract Chemotrophically grown cells of Rhodopseudomonas capsulata contain at least three different pyridine nucleotide dehydrogenases, i) a soluble, found in the supernatant (144000 × g) of cell free extracts, NADH-dependent, ii) a mem brane-bound, NADH-dependent, and iii) a soluble, found in the supernatant N AD PH dependent. The membrane-bound NADH dehydrogenase (E.C. 1.6.99.3) has been solubilized by sodium deoxycholate treatm ent of m em branes and purified 75 fold by column chrom atography on Sephadex G-150 and DEAE cellulose in the presence of sodium cholate. The native enzyme has an apparent molecular mass (Mr) of 97 000, containing polypeptides of Mr of about 15 000. The pH optim um was at 7.5. The enzyme was specific for NADH. The Michaelis constant for NADH and DCIP were 4.0 and 63 μm, respectively. The enzyme was inactivated by FMN, riboflavin and NADH. In contrast, the soluble NADH-dehydrogenase (i) was activated by FMN.


1997 ◽  
Vol 185 (1) ◽  
pp. 210-216 ◽  
Author(s):  
Mitsuko Fujiwara ◽  
Robert H. Grubbs ◽  
John D. Baldeschwieler

Sign in / Sign up

Export Citation Format

Share Document