نتایج جستجو برای: isoenzyme electrophoresis

تعداد نتایج: 54597  

2010
Nori Komatsu Yukiko Ose Akira Kido Masakazu Oya N. Kitahara

Abstrac£: The possibiiity of determination of 6-phosphogluconate dehydrogenase (PGD) types from bloodstains made on filter paper was examined by starch gel electrophoresis. Addition of NADP to the gel and cathodal buffers yielded a rather better visualization of isoenzyme bands. The time limits of determination o£ PGD types were: at 40C 6 weeks, at room temperature 4 weeks, at 370C }ess than l ...

Journal: :Clinical chemistry 1980
J E Buttery C R Milner P Nenadovic P R Pannall

We report another patient with a circulating alkaline phosphatase/immunoglobulin complex in his blood, and describe a simple method of demonstrating such complexes. On electrophoresis on cellulose acetate, the complex was relatively slow moving and there was no activity in the normal bone/liver isoenzyme region. When the serum was treated with trypsin, the slow band disappeared and the normal p...

2005
J. PIERCE ROBERT G. PRICE JOHN S. L. FOWLER

N-Acetyl-fi-D-glucosaminidase activities were determined in homogenates of marmoset kidney, in serum and in urine by using the 4-methylumbelliferyl substrate. The enzyme activity was separated into several components by DEAE-cellulose ion-exchange chromatography, starch-gel electrophoresis and isoelectric focusing. The kidney contained two major forms of the enzyme, A and B, which had similar p...

Journal: :Biochemical Society transactions 1978
S R Reddy D C Watts

carbonic anhydrase III with an estimated purity of greater than 95%, as judged by electrophoresis in sodium dodecyl sulphate/polyacrylamide gels. Ion-exchange chromatography and salt fractionation were used to purify the bovine carbonic anhydrase 111. Bovine muscle was homogenized and adjusted t o 40% saturation with (NH4)*S04. The supernatant was applied t o a DEAE-cellulose column (2.5cm x 25...

Journal: :Clinical chemistry 1975
W G Yasmineh N Q Hanson

We have compared two methods for separating the isoenzymes of creatine kinase in serum and measuring their activity: chromatography on diethylaminoethyl-Sephadex A-50, with both continuous and discontinuous gradient elution, and electrophoresis on cellulose acetate. Results by continuous and discontinuous gradient elution correlated well both for tissue extracts and sera. Electrophoresis on cel...

2004
JIan-Guo Geng

We describe a procedure for purification of creatine kinase (EC 2.7.3.2) MB isoenzyme (CK-MB) from human cardiac muscle by preparative electrophoresis on polyacrylamide gel. From a 50-g portion of human myocardium we isolated 21 mg of CK-MB, which had a specific creatine kinase activity of 405 kU/g. The CK-MB exhibited an enzyme band on polyacrylamide gel electrophoresis (PAGE) with staining fo...

2009
N. Subramanian H. Mohana Krishnan P. Venkatachalam

To establish Lactate dehydrogenase (LDH) isoenzyme is a biochemical tumor marker in cervical carcinoma patients for diagnosis and treatment monitoring of the disease. The Serum and cervical tissue LDH isoenzyme was analyzed qualitatively by Poly Acrylamide Disc Gel Electrophoresis method. The total LDH activity was estimated quantitatively by the method of UV spectrophotometry. 50 untreated cer...

Journal: :Annals of clinical and laboratory science 1984
E Epstein F L Kiechle B Zak

A useful laboratory test for the differentiation of liver, bone, and intestinal alkaline phosphatase (ALP) isoenzymes in serum is presented. Electrophoresis in polyacrylamide gel is performed with untreated serum as well as with serum incubated at 56 degrees C for 10 min. The heating step denatures bone isoenzyme which may obscure the liver ALP band when present in large amounts. Visualization ...

Journal: :European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies 1995
K Tanishima S X Gao R Yamamoto H Yoshida

We assayed the isoenzymes of lactate dehydrogenase (EC 1.1.1.27) in commercial quality control sea and several animal tissue extracts, using electrophoresis. We compared the Km values and activation energies of the isoenzymes, in order to find suitable animal tissue sources with a similar isoenzyme profile to that of human serum lactate dehydrogenase. Some of the control sera contained only one...

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