Two MethodsComparedfor MeasuringLD-liTotaJLD Activityin Serum

نویسنده

  • Larry H. Bernstein
چکیده

We presentevidencefor the utilityof an improvedassay for the activity of lactate dehydrogenase (EC 1.1.1.27) isoenzymes1 and 2 in serum, involvinginhibitionof the H-subunit of LD by pyruvate at pH 7.1. Resultscorrelatewell with the LD-1/total LD ratio as evaluated by immunologicalassay and, as an indexto infarct, the method is superiorto either the change in CK-MB activityor to the LD-1 activity or to a combinationof these tests, as is the percentage of LD-1 to total LD activity. Moreover, the percentage inhibition ofLD activity by pyruvate may have an advantageoverother methods of isoenzyme fractionation because of its smaller populationCV for patientswith acute myocardialinfarction than is true of other methods. We also demonstrate how, usinga lineardiscriminantanalysis,we comparedthismethod with alternativemethods.We determinedthat evaluation ofCK-MB isoenzymecontributesno informationinadditionto that obtainedfrom the LD-1 isoenzyme.

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

The Most-Cited 1987 Physical-Sciences Articles: Superconductivity Supersedes Superstrings

This study of the 100physical-sciencespaperspublishedin 1987and most cited in 1987and 1988 revealsa near totrdpreoccupationwith the revolutionaryadvancesin superconductorsand superconductivityreportedthat year. The levelof activityin this fieldwas so high that it virtnrdlyexcluded otherfieldsof studyfromour Bibliography. Thesubjectsthatordinarilyappearin ourphysical-sciences studies—suchas supe...

متن کامل

Metabolic clock generates nutrient anticipation rhythms in mTOR signaling

The mTOR signaling pathway modulates metabolic processes with respect to nutrient availability and other growth-related cues. According to the existing paradigm, mTOR complex 1 (mTORC1) activityin vivo is induced by food and gradually decreases during fasting. We found that mTORC1 activity is controlled by an internal clock mechanism different from the known light-entrainable circadian clock. W...

متن کامل

Activityin Serumwith Useof the “CentrifiChem”

Acid phosphatase activity is determined by splitting 1-naphthyl phosphate, concurrently diazotizing the released 1-naphthol with Fast Red TR, and measuring the resulting color. The test is performed in the presence and absence of tartrate. Reaction rates can be continuously monitored, and their difference is proportional to acid phosphatase activity that is inhibited by tartrate. Results for se...

متن کامل

Koncentracija Kalcijuma I Fosfora I Aktivnost Alkalne Fosfataze U Serumu Zdrave Dece Tokom Rasta I Razvoja Serum Calciumand Phosphorus Concentration and Alkaline Phosphatase Activityin Healthy Children during Growth and Development

Vise od 99% kalcijuma i 80-85% fosfora ljudskog organizma zastupljeno je u kostima, ali ovi elementi imaju i druge vazne funkcije u organizmu [1]. Najveci deo preostale kolicine kalcijuma nalazi se u plazmi u koncentraciji izmedu 2,25 i 2,75 mmol/\. Iako je kolicina kalcijuma u plazmi relativno mala u odnosu na kolicinu u kostima, ipak je kriticki vazna za regulaciju velikog broja aktivnosti: s...

متن کامل

Direct SpectrophotometricDeterminationof a-Amylase Activityin Saliva, with p-Nitrophenyla-Maltoside as Substrate

We describe a simple, direct kinetic method for determination of salivary a-amylase (1,4 a-o-glucan 4-glucanohydrolase, EC 3.2.1.1). The assay makes use of a well-defined substrate, p-nitrophenyl a-maltoside, which is hydrolyzed by a-amylase to a chromogenic product, p-nitrophenol. Activity is determined by directly monitoring the increase in absorbance of the reaction mixture. Amylase activity...

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:

دوره   شماره 

صفحات  -

تاریخ انتشار 2004