Lactic dehydrogenase inhibitors in NAD.

نویسندگان

  • A L Babson
  • E G Arndt
چکیده

The vacuum oven-drying method (60#{176}C) was compared with the freeze-drying method. By the former method, 72.85 ± 0.0374 (SD) % moisturewas removed, by thelatter, 81.04 ± 0.050%.The feces were from the same source. With the freeze-drying method total moisture removed is clearly greater, and the time required was only 16 h, as compared with 48 h required by the vacuum oven-drying method. There are other distinct advantages. Since measurement of the total energy of the sample is based on a rise in temperature at the point of combustion,freeze-drying duringpreparation eliminates any possibility of a rise in temperature that might lead to an error in calculating the total energy. Drying to a constant weight, which necessitates timeconsuming multipleweighings,is not required.The driedsample isintheform ofa powder and requiresno grinding. Unpleasant odors associated with the ovendrying method are avoided. To bettercompare the old oven-drying method and the new freeze-drying method, caloricontentof four specimens ofthesame sampleoffeceswas measured by each method. The results were in good agreement (Table 1). The results shown in Table 1 for the wet weight in kilogram-calories per gram are calculated by multiplying the dry weight (kcal/g) by the percent remaining moisture (100% minus the percent moisture removed). We feel that this method represents a distinct improvement over the original methods.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Preliminary Report of NAD+-Dependent Amino Acid Dehydrogenase Producing Bacteria Isolated from Soil

Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the reversible oxidative deamination of an amino acid to its keto acid and ammonia with the concomitant reduction of either NAD+, NADP+ or FAD. These enzymes have been received much attention as biocatalysts for use in biosensors or diagnostic kit...

متن کامل

Influence of carboxylic acids on the stereospecific nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lactate dehydrogenases of Leuconostoc mesenteroides.

Leuconostoc mesenteroides increased its lactic acid production from glucose threefold when malic acid was added to the culture. This increase resulted also in a reduction of the ratio of d-lactic acid to l-lactic acid (31.5 to 1.23). Addition of malic acid increased 6.5-fold the specific activity of nicotinamide adenine dinucleotide (NAD)-linked l-lactate dehydrogenase and increased 3.2-fold th...

متن کامل

Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors.

Inhibitors of human lactate dehydrogenase (hLDH5)-the enzyme responsible for the conversion of pyruvate to lactate coupled with oxidation of NADH to NAD⁺-are promising therapeutic agents against cancer because this enzyme is generally found to be overexpressed in most invasive cancer cells and is linked to their vitality especially under hypoxic conditions. Consequently, significant efforts hav...

متن کامل

Activity of select dehydrogenases with Sepharose-immobilized N6-carboxymethyl-NAD

N(6)-carboxymethyl-NAD (N(6)-CM-NAD) can be used to immobilize NAD onto a substrate containing terminal primary amines. We previously immobilized N(6)-CM-NAD onto sepharose beads and showed that Thermotoga maritima glycerol dehydrogenase could use the immobilized cofactor with cofactor recycling. We now show that Saccharomyces cerevisiae alcohol dehydrogenase, rabbit muscle L-lactate dehydrogen...

متن کامل

58. Crystalline Lactic Dehydrogenase from Heart Muscle

THE reduction of methylene blue by lactic acid, or in other words, the dehydrogenation of lactic acid in the presence of extracts from animal tissues, is now known to be catalysed by a system composed of two enzymes (lactic dehydrogenase and diaphorase flavoprotein) and cozymase [Dewan & Green, 1938; Euler & Hellstrom, 1938]. The chemical reactions involved in this process may be written [Corra...

متن کامل

Properties of Malolactic Activity Purified from Leuconostoc oenos ML34 by Affinity Chromatography.

Malolactic activity from Leuconostoc oenos ML34 is tightly associated with lactic dehydrogenase. A simple and fast procedure, involving affinity chromatography on agarose-hexane-NAD (Agnad), was used to separate malolactic activity from lactic dehydrogenase and other proteins. The yield was ca. 86%, the purification was 5.2-fold, and the K(m) values for l-malate, NAD and Mn were 2.8, 0.13, and ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Clinical chemistry

دوره 16 3  شماره 

صفحات  -

تاریخ انتشار 1970