The thin-layer isoelectric focusing of lactate dehydrogenase isoenzymes in rabbit lens parts and in intraocular tissues

1977 ◽  
Vol 203 (1) ◽  
pp. 9-19 ◽  
Author(s):  
J. Bours ◽  
H. Neuhaus ◽  
O. Hockwin
Keyword(s):  
Lactate Dehydrogenase ◽  
Thin Layer ◽  
Isoelectric Focusing ◽  
Rabbit Lens ◽  
Lactate Dehydrogenase Isoenzymes

Separation of turkey lactate dehydrogenase isoenzymes using isoelectric focusing technique

2015 ◽  
Vol 37 (2) ◽  
pp. 335-338 ◽  
Author(s):  
Dagmar Heinová ◽  
Zuzana Kostecká ◽  
Tomáš Csank
Keyword(s):  
Lactate Dehydrogenase ◽  
Isoelectric Focusing ◽  
Lactate Dehydrogenase Isoenzymes

Accuracy of lactate dehydrogenase isoenzyme estimations by a thin-layer agarose fluorescent technique: experience with ternary and quaternary mixtures of purified human lactate dehydrogenase isoenzymes.

1983 ◽  
Vol 29 (12) ◽  
pp. 2096-2099
Author(s):  
E M Pridgar ◽  
F Y Leung ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Thin Layer ◽  
Binary Mixtures ◽  
Peak Height ◽  
Clin Pathol ◽  
Dehydrogenase Isoenzyme ◽  
Fluorescent Technique ◽  
Lactate Dehydrogenase Isoenzymes

Abstract We have further assessed the accuracy of the thin-layer agarose fluorescent technique of Elevitch et al. [Am J Clin Pathol 46, 692 (1966)]. Previously, we used semi-purified human lactate dehydrogenase isoenzyme-1 and -5 [Clin Chem 22, 1995 (1976)] and isoenzyme-1 and -2 [Clin Chem 27, 1708 (1981)] to show that this assay accurately measures the proportions of these binary mixtures. In the present study, using ternary and quaternary mixtures of isoenzyme- 1, -2, -3, and -5, we show that the assay gives accurate estimations of all of these isoenzymes, within the errors of the techniques used. We also show that peak area (integration) is more nearly accurate, but less precise, than peak height (amplitude) measurements.

scholarly journals How accurate are lactate dehydrogenase isoenzyme estimations by the thin-layer agarose fluorescent technique?

1976 ◽  
Vol 22 (12) ◽  
pp. 1995-1998 ◽  
Author(s):  
D McKenzie ◽  
P I Clark ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Thin Layer ◽  
Unbiased Estimate ◽  
Clin Pathol ◽  
Dehydrogenase Isoenzyme ◽  
Fluorescent Technique ◽  
Definitive Method ◽  
Lactate Dehydrogenase Isoenzymes

Abstract We offer an assessment of the accuracy of the thin-layer agarose fluorescent technique of Elevitch et al. [Am. J. Clin. Pathol. 46, 692 (1966)]. We used semi-purified human lactate dehydrogenase isoenzymes 1 and 5. Both the lactate lead to pyruvate and pyruvate lead to lactate assays [Clin. Chem. 20, 1462 (1974)] appear to give, within the errors of the techniques used, a substantially unbiased estimate of both LD-1 and LD-5, although this must remain a provisional conclusion until a definitive method of assay for the total and isoenzymic LD activities is created. Introducing a buffer into the substrate mixture (lactate lead to pyruvate assay) had no effect on these findings except at extremes of pH, when marked inaccuracies occurred.

Purification of lactate dehydrogenase isoenzymes one, two, and three from human erythrocytes.

1984 ◽  
Vol 30 (8) ◽  
pp. 1353-1357 ◽  
Author(s):  
E M Pridgar ◽  
G C Moses ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Ion Exchange ◽  
Thin Layer ◽  
Sodium Lauryl Sulfate ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Erythrocytes ◽  
Lauryl Sulfate ◽  
Specific Activities ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Lactate dehydrogenase (LD) isoenzymes 1, 2, and 3 were prepared from human erythrocytes by sequential ion-exchange chromatography followed by general-ligand (AMP analog) affinity chromatography. Respective yields, purification factors, and specific activities (kU per gram of protein) were 25%, 4394-fold, and 209.7; 40% 4385-fold, and 199.1; and 18%, 7565-fold, and 192.9. The respective preparations contained less than 0.5% of contaminating LD isoenzyme activity as judged from electrophoresis on thin-layer agarose, were homogeneous as judged by electrophoresis on polyacrylamide gel (both in the presence and absence of sodium lauryl sulfate), and showed minor contamination by other LD isoenzymes as judged by analytical isoelectric focusing. We think that these preparations would be useful as human-based calibrating or reference materials. Their purity is such that these preparations could also be used as antigens for the development of suitable antisera.

Characterization of free and tightly bound lipoprotein in intima by thin layer isoelectric focusing

1979 ◽  
Vol 33 (3) ◽  
pp. 329-342 ◽  
Author(s):  
Elspeth B. Smith ◽  
Heather S. Dietz ◽  
Isobel B. Craig
Keyword(s):  
Thin Layer ◽  
Isoelectric Focusing

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

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