نتایج جستجو برای: isoenzyme electrophoresis

تعداد نتایج: 54597  

2012
J. E

1. Changes in the perfusate activities of aspartate transaminase, lactate dehydrogenase, its ‘LD-5’ component, sorbitol dehydrogenase, ornithine carbamoyltransferase, and the isoenzyme patterns of lactate dehydrogenase and aspartate transaminase, were investigated in eleven perfusions of pig liver with human blood in order to assess liver cell damage during perfusion. 2. The aspartate transamin...

Journal: :Clinical chemistry 1980
P J Langlais W J McEntee E D Bird

The intestinally derived isoenzyme of alkaline phosphatase (ALP; EC 3.1.3.1) in serum is easily differentiated from other isoenzymes by electrophoresis on either starch, acrylamide, agar or agarose gels, or cellulose acetate membranes. In general, these techniques are not quantitative, but differential-inhibition techniques allow one to estimate the activity of the intestinal isoenzyme. LPhenyl...

Journal: :Clinical chemistry 1984
T H Massey M R Goe

We studied the transient appearance of creatine kinase (EC 2.7.3.2) isoenzyme BB, as measured by electrophoresis, in serum or plasma from 19 patients who had just experienced cardiac or respiratory arrest. Creatine kinase BB activity was greatest 0.5 to 3 h after the arrest, with values (measured at 30 degrees C) ranging from 3 to 27 U/L (mean, 7.8 U/L) in 18 patients who were successfully resu...

Journal: :Journal of clinical pathology 1986
M D Shephard M J Peake R N Walmsley

A method for quantitating the liver, bone, intestinal and placental alkaline phosphatase activity of serum, using an algorithm for converting selective inactivation by guanidine hydrochloride, L-phenylalanine, and heat into equivalent isoenzyme activity is described. The method can individually quantify mixtures of isoenzymes to within a margin of 3%; it has acceptable reproducibility and has b...

Journal: :Clinical chemistry 1974
T O Tiffany J M Parella W F Johnson C A Burtis

The MB isoenzyme of creatine kinase (EC 2.7.3.2) may be prepared in vitro by dissociation of the MM and BB dimers into the M and B monomers. These monomers then recombine in a random manner to form all possible combinations-MM, MB, and BBthe presence of which may be detected by chromatography or electrophoresis. Dawson et al. (1) describe this process for animal tissues, while Keutel et a!. (2)...

Journal: :Plant physiology 1990
E M McMorrow J W Bradbeer

The chloroplast and cytoplasmic isoenzymes of phosphoglycerate kinase (PGK) (EC. 2.7.2.3) from Hordeum vulgare leaves have been separated and purified for the first time to apparent homogeneity. The method for purifying the isoenzymes is described here and consists of DEAE Sephacel chromatography followed by affinity chromatography on ATP Sepharose. This consistently provided a 500- to 900-fold...

Journal: :Annals of tropical medicine and parasitology 1999
T Chavez J Moreno J P Dujardin

Seventeen samples of Rhodnius, representing at least eight different species according to their morphological characteristics, were submitted to multilocus isoenzyme electrophoresis, revealing 17 different loci. A phenetic analysis of the enzyme data not only clustered the species in accordance with their geographical origin but also revealed interspecific relationships that differed from those...

Journal: :The British journal of ophthalmology 1976
I L Kahán K Juhász

The lactate dehydrogenase isoenzyme patterns in 46 extraocular eye muscle samples removed at surgery for squint were determined by acrylamide-gel electrophoresis and reduction of NAD coupled with formazan reaction. Muscle type subunits predominated in the isoenzymes of the medial and lateral rectus muscles of emmetropic and hypermetropic eyes, whereas heart type subunits predominated in those o...

Journal: :Clinical chemistry 1984
S B Rosalki A Y Foo

We describe two new methods for the separation and quantification of the bone and liver isoenzymes of alkaline phosphatase (EC 3.1.3.1) in plasma. In the first, we use wheat-germ lectin to precipitate the bone isoenzyme. About 80% of this, but minimal liver isoenzyme, is precipitated. The activity of the bone isoenzyme is calculated from measuring the alkaline phosphatase activity in the precip...

Journal: :The Biochemical journal 1976
T Noguchi Y Minatogawa E Okuno R Kido

The organ distribution of rat histidine-pyruvate aminotransferase isoenzymes 1 and 2 was examined by using an isoelectric-focusing technique. Isoenzyme 1 (pI8.0) is present only in the liver and its activity is increased by the injection of glucagon, whereas isoenzyme 2 (pI5.2) is distributed in all tissues (liver, kidney, brain and heart) tested, and is not affected by glucagon injection. Isoe...

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