scholarly journals Effect of chlorocamphene on the isoenzyme spectrum of lactate dehydrogenase in rat serum and liver.

1976 ◽  
Vol 13 ◽  
pp. 127-132 ◽  
Author(s):  
U A Kuz'minskaya ◽  
S M Alekhina
Keyword(s):  
Lactate Dehydrogenase ◽  
Rat Serum ◽  
Isoenzyme Spectrum

Total lactate dehydrogenase and its isoenzymes in serum in the presence of penicillamine and other sulfhydryl compounds.

1977 ◽  
Vol 23 (2) ◽  
pp. 229-233 ◽  
Author(s):  
L L Gershbein ◽  
K G Raikoff
Keyword(s):  
Lactate Dehydrogenase ◽  
Disc Electrophoresis ◽  
The Other ◽  
Rat Serum ◽  
Initial Concentration ◽  
Ldh Isoenzymes ◽  
Allosteric Effectors ◽  
Sulfhydryl Compounds

Abstract Toward delineation of changes in total lactate dehydrogenase (LDH) and in the distribution of LDH isoenzymes as assessed by polyacrylamide disc electrophoresis, we inbucated human and rat sera with various agents, notably sulfhydryl compounds. Although artefacts were apparent when these agents were used without preliminary adjustment of pH, we saw little alteration in total unitage when one or two volumes of serum was mixed with one volume of any of several thiols, especially penicillamine, at an initial concentration of 0.4 mol/liter and pH 7.0-7.5. Under these conditions, penicillamine caused a loss in LDH-5 after incubation for 1 h at 25 degrees C together with small decreases in mobility of the other four isoenzymes toward the anode. A zymosan region appeared below the albumin and tracking dye area. With longer periods of incubation of rat serum with penicillamine or alpha-mercaptosuccinate, a novel band in the zymogram was noted just above the LDH-4 peak. The observations are discussed in terms of allosteric effectors.

Blood Platelets as a Possible Source of Creatine Kinase in Rat Plasma and Serum

1978 ◽  
Vol 39 (03) ◽  
pp. 701-706 ◽  
Author(s):  
Sachiko Shibata ◽  
Bonro Kobayashi
Keyword(s):  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Blood Platelets ◽  
Rat Plasma ◽  
Muscle Type ◽  
Rat Serum ◽  
Old Rats ◽  
The Brain

SummaryThe creatine kinase (CK) activity in rat plasma was found to be correlated with that in serum or platelets. Rat serum contained higher activity not only of CK but also of lactate dehydrogenase than the corresponding plasma. The plasma CK activity decreased with increasing age of rats. Only the brain-type isoenzyme of CK was found in plasma, serum and platelets. Contamination of brain-type with muscle-type isoenzyme was detected in rather exceptional cases in which the activity was high among old rats. These results suggest the possible contribution of blood platelets to the CK activity of circulating plasma as well as to the activity in serum in rats.

scholarly journals Polymorphism of lactate dehydrogenase B subunit in rat erythrocytes

1985 ◽  
Vol 45 (1) ◽  
pp. 101-106 ◽  
Author(s):  
V. Stolc
Keyword(s):  
Lactate Dehydrogenase ◽  
Regulator Gene ◽  
Rat Erythrocytes ◽  
Rat Serum ◽  
Glyoxalase 1 ◽  
B Subunit ◽  
Coat Pattern ◽  
A Subunit

SummaryLactate dehydrogenase regulator gene Ldr-1 controls the amount of the lactate dehydrogenase A subunit in rat serum and the amount of lactate dehydrogenase B subunit in rat erythrocytes because no recombinant rats were found among 295 pups produced in the BDIV × (ACI × BDIV)F1 and (ACI × DI) Fl × DI backcrosses. Two alleles regulate the high (Ldr-1a) and low (Ldr-1b) activity enzyme. The Ldr-1 is not linked to hooded coat pattern or glyoxalase-1. Sex and Ldr-1 assorted independently; hence the gene is autosomal.

Serum Lactate Dehydrogenase Isoenzyme 1 and Relapse in Patients with Nonseminomatous Testicular Germ Cell Tumors Clinical Stage I

2001 ◽  
Vol 40 (4) ◽  
pp. 536-540 ◽  
Author(s):  
Finn Edler von Eyben ◽  
Ebbe Lindegaard Madsen ◽  
Ole Blaabjerg ◽  
Per Hyltoft Petersen ◽  
Hans von der Maase ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Germ Cell ◽  
Clinical Stage ◽  
Germ Cell Tumors ◽  
Serum Lactate ◽  
Stage I ◽  
Serum Lactate Dehydrogenase ◽  
Testicular Germ Cell Tumors ◽  
Testicular Germ Cell ◽  
Dehydrogenase Isoenzyme

FUNCTIONAL HETEROGENEITY OF THE THYROID AND POSSIBLE PRESENCE OF IODOTYROSINE-LIKE COMPOUNDS IN NORMAL SERUM

1965 ◽  
Vol 48 (2) ◽  
pp. 199-208 ◽  
Author(s):  
J. D. Wiener
Keyword(s):  
Human Subjects ◽  
Thyroid Tissue ◽  
Normal Serum ◽  
Schematic Model ◽  
Functional Heterogeneity ◽  
Rat Serum ◽  
Iodine Metabolism ◽  
Normal Rat ◽  
Isotope Equilibrium ◽  
Equilibrium Experiment

ABSTRACT After the administration of 131I to normal animals or human subjects, labelled thyroxine and triiodothyronine, but at most traces of labelled iodotyrosines can be detected in the serum. However, several investigators using various methods claim to have found considerable amounts of one or both of these iodotyrosines when assaying the stable (non-radioactive) iodinated compounds in the serum. Considering the available evidence as convincing for the present, an attempt has been made to explain this discrepancy. A schematic model of the thyroidal iodine metabolism is proposed, based on (a) the hypothesis that the iodotyrosines are present in the circulation in a »masked« form (i. e. protected against deiodination), and (b) the known functional heterogeneity of the thyroid tissue. This heterogeneity should be of a qualitative as well as quantitative nature. As the physical decay rate of 131I is short in comparison with the turnover rate of the masked iodotyrosine pool, an isotope equilibrium experiment with rats was carried out, using the long-lived isotope 125I. The results of this experiment, viewed together with those of a similar investigation published by others, seem to lend support to the proposed mechanism. The presence of non-negligible amounts of a diiodotyrosine-like compound in normal rat serum seems fairly well established.

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