Separation of Creatine Kinase Isoenzymes in Serum by Ion-Exchange Column Chromatography (Mercer's Method, Modified to Increase Sensitivity)

1975 ◽  
Vol 21 (3) ◽  
pp. 392-397 ◽  
Author(s):  
Daniel A Nealon ◽  
Arthur R Henderson

Abstract We describe our experience with Mercer's method [Clin. Chem. 20, 36 (1974)] for separating isoenzymes of creatine kinase (EC 2.7.3.2) in serum by ion-exchange chromatography. By using diethylaminoethyl cellulose rather than diethylaminoethyl Sephadex in the column and by changing the ionic strength of the eluting buffer, we could detect a significant proportion of the MB isoenzyme of serum creatine kinase at normal activities of creatine kinase in serum, even in the absence of cardiac disease.

1993 ◽  
Vol 48 (12) ◽  
pp. 1727-1731 ◽  
Author(s):  
A. Franken ◽  
W. Preetz ◽  
M. Rath ◽  
K.-F. Hesse

By electrochemical oxidation of [B6H6]2- in the presence of nitrite ions and the base DBU in dichloromethane solution mononitropentahydrohexaborate [B6H5(NO2)]2- ions are formed and can be isolated by ion exchange chromatography on diethylaminoethyl cellulose. The crystal structures of the K and Cs salt were determined from single crystal X-ray diffraction analyses. K2[B6H5(NO2)] is monoclinic, space group P21/m with a = 5.953(1), b = 8.059(4), c = 8.906(1) Å, β = 109.553(9)°; Cs2[B6H5(NO2)] is monoclinic, space group P21/a with a = 9.438(6), b = 9.644(7), c = 11.138(9) Å, β = 101.44(9)°. The B6 octahedron is compressed in the direction of the B—NO2 bond by about 5%, with bond lengths between 1.67 and 1.77 A.


1994 ◽  
Vol 49 (9) ◽  
pp. 1263-1266 ◽  
Author(s):  
A. Franken ◽  
W. Preetz

By electrochemical oxidation of [B6H6]2- in the presence of nitrite ions and of the base DBU in dichlorom ethane solution the μ-nitroso-bis(pentahydrohexaborate) [B6H5(NO)B6H5]3- ion is formed and can be isolated by ion exchange chromatography on diethylaminoethyl cellulose. The crystal structure of the Cs salt has been determined from single crystal X-ray diffraction analysis. Cs3[B6H5(NO)B6H5] is orthorhombic, space group Pnma with a = 16.2303(13), b = 12.245(6), c = 25.444(2) Å. The unit cell contains three crystallographically independent anions with nearly C2v symmetry but differently distorted B6 cages


1980 ◽  
Vol 35 (8) ◽  
pp. 994-999 ◽  
Author(s):  
G. Peters ◽  
W. Preetz

Abstract From the system of isomeric complex ions [Os(NCS)n(SCN)6-n]3-, 9 of 10 possible species, n = 1-6, are isolated, including for n = 2, 3, 4 the first representatives of pure geometric bond isomers. By reaction of K2[OsCl6] with aqueous KSCN solution at reflux temperature, trans(mer)-complexes, and on treatment at 60 °C exclusively cis(fac)- complexes are formed. By ion exchange chromatography on diethylaminoethyl-cellulose columns, from mixtures of pairs of geometric isomers the pure trans(mer)-compounds are enriched in front, the cis(fac)-species at the end of the zones. Characterization and assignment of the configuration of the geometric isomers is based upon the reproducible differences in the IR and Raman spectra.


1984 ◽  
Vol 39 (9) ◽  
pp. 1185-1192 ◽  
Author(s):  
D. Tensfeldt ◽  
W. Preetz

The reaction of [IrCl6]2- with BrF3 generates the mixed complexes [IrFnCl6-n]2-, n = 1-5, of which the species with n = 2, 3, 4 are ds-configurated. Due to the stronger trans-effect of Cl as compared to F on treatment of [IrF5Cl]2- and cis-[IrF4Cl2]2- with SOCl2 the trans-isomers are formed stereospecifically. The pure fluoro-chloro-iridates(IV) are separated by ion exchange chromatography on diethylaminoethyl-cellulose. The vibrational spectra of the mixed ligand complexes are completely assigned according to point groups D4h, C4v, C3v, and C2v. The IrCl stretching vibration of [IrF5Cl]2- is split by the isotopes 35C1 and 37Cl, showing two well resolved sharp Raman lines at 361 and 355 cm-1.


1980 ◽  
Vol 26 (8) ◽  
pp. 1209-1212 ◽  
Author(s):  
P G Rand ◽  
C Nelson

Abstract The accuracy of many convenient methods for determining the proportion of hemoglobin AI to total hemoglobin by ion-exchange chromatography is in question because those methods have not been evaluated against a reference method. In addition, several if not all of these tests are influenced by laboratory temperature. We modified the chromatographic conditions usually used, to arrive at a method that gives results that agree well with those by the Trivelli method (N. Engl. J. Med. 284, 353, 1971) and is less influenced by ambient temperature than are results obtained with the commercially available Helena and Isolab kits. We accomplished this by lowering the pH of the fast-hemoglobin eluting buffer, with a corresponding adjustment in the ionic strength. We also use a larger elution volume, which assures more nearly complete elution of the hemoglobin A1 fraction. The final method (y) agreed being y = 0.98x + 0.63 r2 = 0.887. Average results from the Helena and Isolab methods were lower than with the reference method by 1.58 and 3.03% hemoglobin A1, respectively.


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