The activity of lactate dehydrogenase of the supernatant fraction of brain, heart, skeletal muscle, and liver of l-day and 4-, 12-, 30-, 74-, and 96-week old rats was determined to study the changes in this enzyme with increasing age. Units of enzyme per g, wet weight, of all the tissues increased during the growth phase, reaching a maximum at 30 weeks, and then decreased. NADH,:NADHn ratios, K...

1. Papadopoulos, N. M., and Hufnagel, C. A., Evaluation of lactate dehydrogenase isoenzyme patterns in serum of patients undergoing cardiac surgery. J. Thorac. Cardiovasc. Surg. 76, 173-177 (1978). 2. McKenzie, D., Clarke, P. I., and Henderson, A. R., How accurate are lactate dehydrogenase isoenzyme estimations by the thin-layer agarose fluorescent technique? Clin. Chem. 22, 1995-1998 (1976). 3...

1. Papadopoulos, N. M., and Hufnagel, C. A., Evaluation of lactate dehydrogenase isoenzyme patterns in serum of patients undergoing cardiac surgery. J. Thorac. Cardiovasc. Surg. 76, 173-177 (1978). 2. McKenzie, D., Clarke, P. I., and Henderson, A. R., How accurate are lactate dehydrogenase isoenzyme estimations by the thin-layer agarose fluorescent technique? Clin. Chem. 22, 1995-1998 (1976). 3...

Activity of D-lactate dehydrogenase (D-LDH) was shown not only in cell extracts from Megasphaera elsdenii grown on DL-lactate, but also in cell extracts from glucose-grown cells, although glucose-grown cells contained approximately half as much D-LDH as DL-lactate-grown cells. This indicates that the D-LDH of M. elsdenii is a constitutive enzyme. However, lactate racemase (LR) activity was pres...

Anaerobically, Brochothrix thermosphacta fermented glucose primarily to l-lactate, acetate, formate, and ethanol. The ratio of these end products varied with growth conditions. Both the presence of acetate and formate and a pH below about 6 increased l-lactate production from glucose. Small amounts of butane-2,3-diol were also produced when the pH of the culture was low (</=5.5) or when acetate...

Cell-free extracts of Chlorella pyrenoidosa contained two enzymes capable of oxidizing d-lactate; these were glycolate dehydrogenase and NAD(+)-dependent d-lactate dehydrogenase. The two enzymes could be distinguished by differential centrifugation, glycolate dehydrogenase being largely particulate and NAD(+)-d-lactate dehydrogenase being soluble. The reduction of pyruvate by NADH proceeded mor...

1. Kinetic data concerning the substrate and product inhibition by pyruvate and L-lactate have been obtained with the Md and Hd fractions separated from crystalline rabbit muscle lactic dehydrogenase. 2. The studies indicate that the product inhibition by L-lactate or by pyruvate is predominantly noncompetitive for both the Mq and Hq isozymes. Ki values for product inhibition by L-lactate were ...

how to cite this article: khosroshahi n, alizadeh p, khosravi m, salamati p, kamrani k. spinal fluid lactate dehydrogenase level differentiates between structural and metabolic etiologies of altered mental status in children. iran j child neurol. 2015 winter;9(1):31-36. abstract objective altered mental status is a common cause of intensive care unit admission in children. differentiating struc...

Lactate dehydrogenase (LD: EC 1.1.1.27) is the most important clinically of several dehydrogenases occurring in human serum. Lactate dehydrogenase is cytoplasmic in its cellular location and in any one tissue is composed of one or two of five possible isoenzymes. While many of its clinical applications involve quantification of one or more specific serum isoenzymes, an estimate of total LD is r...