scholarly journals Glutathione transferase isoenzymes from human prostate

1990 ◽  
Vol 271 (2) ◽  
pp. 481-485 ◽  
Author(s):  
C Di Ilio ◽  
A Aceto ◽  
T Bucciarelli ◽  
S Angelucci ◽  
M Felaco ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Immunohistochemical Staining ◽  
Human Liver ◽  
Glutathione Transferase ◽  
Human Prostate ◽  
Immunoblotting Analysis ◽  
Qualitative And Quantitative ◽  
Quantitative Expression ◽  
Close Relationship ◽  
Liver And Kidney

By using affinity-chromatography and isoelectric-focusing techniques, several forms of glutathione transferase (GSTs) were resolved from human prostate cytosol. All the three major classes of GST, i.e. Alpha, Mu and Pi, are present in human prostate. However, large inter-individual variation in the qualitative and quantitative expression of different isoenzymes resulted in the samples investigated. The most abundant group of prostate isoenzymes showed acid (pI 4.3-4.7) behaviour and were classified as Pi class GSTs on the basis of their immunological and structural properties. Immunohistochemical staining of Pi class GSTs was prevalently distributed in the epithelial cells surrounding the alveolar lumen. Class Mu GSTs are also expressed, although in small amounts and in a limited number of samples, by human prostate. The major cationic isoenzyme purified from prostate, GST-9.6; (pI 9.6; apparent subunit molecular mass of 28 kDa), appears to be different from the cationic GST alpha-epsilon forms isolated from human liver and kidney as evidenced by its structural, kinetical and immunological properties. This enzyme, which accounts for about 20-30% (on protein basis) of total amount of GSTs, is expressed by only 40% of samples. GST-9.6 has the ability to cross-react in immunoblotting analysis with antisera raised against rat liver GST 2-2, rather than with antisera raised against members of human Alpha, Mu and Pi class GSTs. Although prostate GST-9.6 shows close relationship with the human skin GST pI 9.9, it does not correspond to any other known human GST.

Freezing Tolerance in Rhododendron and Its Association with Dehydrin Expression

HortScience ◽  
1998 ◽  
Vol 33 (3) ◽  
pp. 453b-453
Author(s):  
Chon C. Lim ◽  
Stephen L. Krebs ◽  
Rajeev Arora
Keyword(s):  
Normal Distribution ◽  
Cold Acclimation ◽  
Isoelectric Focusing ◽  
Freezing Tolerance ◽  
Cold Hardiness ◽  
Physiological Age ◽  
Western Blots ◽  
Qualitative And Quantitative ◽  
Quantitative Expression ◽  
Cultivar Group

This study examines whether dehydrin expression in leaves is associated with varying levels of cold hardiness among evergreen rhododendrons. Initially, differences in leaf freezing tolerance (LFT) were determined within three groups of plants: 1) a cultivar group; `Chionoides' (CND), `Grumpy Yellow' (GY), and `Vulcan's Flame' (VF) 2) a segregating F2 population derived from a super coldhardy (R. catawbiense) × less-hardy (R. fortunei) cross, and 3) juvenile seedlings and mature plants of wild-collected R. maximum. LFTs in fully acclimated cultivars corresponded with their USDA hardiness zone ratings—CND (zone 4, –32 °C) GY (zone 7, –16 °C), and VF (zone 6, –19 °C). F2 segregation was characterized by a continuous, normal distribution of LFT values, with groups of progeny at the “tails” differing in their mean LFT by 20 °C. Juvenile seedlings of R. maximum exhibited LFTs that were 12 °C lower than LFTs from mature plants. Western blots of leaf proteins revealed a common 50-kDa dehydrin that accumulated during cold acclimation in all three cultivars and appeared to be quantitatively associated with LFTs. Isoelectric focusing of the 50-kDa Rhododendron dehydrin revealed two isoforms (pI 5.5 and 6.5). The more acidic isoform was detected only in the hardiest (CND) cultivar. Experiments are underway to examine qualitative and quantitative expression of dehydrins and its association with LFT in the segregating F2 population and in the group of R. maximum plants differing in physiological age.

scholarly journals Isoelectric focusing of glutathione S-transferases from rat liver and kidney

1978 ◽  
Vol 175 (3) ◽  
pp. 937-943 ◽  
Author(s):  
Barbara F. Hales ◽  
Valerie Jaeger ◽  
Allen H. Neims
Keyword(s):  
Substrate Specificity ◽  
Isoelectric Focusing ◽  
Transferase Activity ◽  
Sprague Dawley ◽  
Substrate Specificities ◽  
Liver Cytosol ◽  
Sprague Dawley Rats ◽  
Isoelectric Points ◽  
Liver And Kidney ◽  
Glutathione S Transferases

The glutathione S-transferases that were purified to homogeneity from liver cytosol have overlapping but distinct substrate specificities and different isoelectric points. This report explores the possibility of using preparative electrofocusing to compare the composition of the transferases in liver and kidney cytosol. Hepatic cytosol from adult male Sprague–Dawley rats was resolved by isoelectric focusing on Sephadex columns into five peaks of transferase activity, each with characteristic substrate specificity. The first four peaks of transferase activity (in order of decreasing basicity) are identified as transferases AA, B, A and C respectively, on the basis of substrate specificity, but the fifth peak (pI6.6) does not correspond to a previously described transferase. Isoelectric focusing of renal cytosol resolves only three major peaks of transferase activity, each with narrow substrate specificity. In the kidney, peak 1 (pI9.0) has most of the activity toward 1-chloro-2,4-dinitrobenzene, peak 2 (pI8.5) toward p-nitrobenzyl chloride, and peak 3 (pI7.0) toward trans-4-phenylbut-3-en-2-one. Renal transferase peak 1 (pI9.0) appears to correspond to transferase B on the basis of pI, substrate specificity and antigenicity. Kidney transferase peaks 2 (pI8.5) and 3 (pI7.0) do not correspond to previously described glutathione S-transferases, although kidney transferase peak 3 is similar to the transferase peak 5 from focused hepatic cytosol. Transferases A and C were not found in kidney cytosol, and transferase AA was detected in only one out of six replicates. Thus it is important to recognize the contribution of individual transferases to total transferase activity in that each transferase may be regulated independently.

scholarly journals Degradation of keratan sulphate by β-N-acetylhexosaminidases A and B

1981 ◽  
Vol 193 (3) ◽  
pp. 811-818 ◽  
Author(s):  
T Ludolph ◽  
E Paschke ◽  
J Glössl ◽  
H Kresse
Keyword(s):  
Isoelectric Focusing ◽  
Human Liver ◽  
Thermal Inactivation ◽  
Sandhoff Disease ◽  
Chromogenic Substrate ◽  
Polymeric Substrate ◽  
Keratan Sulphate ◽  
Human Enzyme ◽  
Tay Sachs Disease

Enzymic cleavage of beta-N-acetylglucosamine residues of keratan sulphate was studied in vitro by using substrate a [3H]glucosamine-labelled desulphated keratan sulphate with N-acetylglucosamine residues at the non-reducing end. Both lysosomal beta-N-acetylhexosaminidases A and B are proposed to participate in the degradation of keratan sulphate on the basis of the following observations. Homogenates of fibroblasts from patients with Sandhoff disease, but not those from patients with Tay–Sachs disease, were unable to release significant amounts of N-acetyl[3H]glucosamine. On isoelectric focusing of beta-N-acetylhexosaminidase from human liver the peaks of keratan sulphate-degrading activity coincided with the activity towards p-nitrophenyl beta-N-acetylglucosaminide. A monospecific antibody against the human enzyme reacted with both enzyme forms and precipitated the keratan sulphate-degrading activity. Both isoenzymes had the same apparent Km of 4mM, but the B form was approximately twice as active as the A form when compared with the activity towards a chromogenic substrate. Differences were noted in the pH–activity profiles of both isoenzymes. Thermal inactivation of isoenzyme B was less pronounced towards the polymeric substrate than towards the p-nitrophenyl derivative.

Cold- and Cryopreservation of Human Liver and Kidney Slices

Cryobiology ◽  
1993 ◽  
Vol 30 (3) ◽  
pp. 250-261 ◽  
Author(s):  
Robyn L. Fisher ◽  
Steven J. Hasal ◽  
Jeffery T. Sanuik ◽  
Katherine S. Scott ◽  
A.Jay Gandolfi ◽  
...  
Keyword(s):  
Human Liver ◽  
Kidney Slices ◽  
Liver And Kidney

Measurements of ultrasonic backscatter coefficients in human liver and kidney in vivo

1995 ◽  
Vol 98 (4) ◽  
pp. 1852-1857 ◽  
Author(s):  
Keith A. Wear ◽  
Brian S. Garra ◽  
Timothy J. Hall
Keyword(s):  
Human Liver ◽  
Liver And Kidney ◽  
Ultrasonic Backscatter

scholarly journals Characterization of antibody against human liver guanase by immunoblotting and immunohistochemical staining of human liver guanase by a direct labeling antibody-enzyme method.

1989 ◽  
Vol 37 (5) ◽  
pp. 611-615 ◽  
Author(s):  
S Ito ◽  
A Iwasaki ◽  
J Syundo ◽  
Y Tamura ◽  
S Kishi ◽  
...  
Keyword(s):  
Liver Enzyme ◽  
Specific Antibody ◽  
Immunohistochemical Staining ◽  
Human Liver ◽  
Liver Extract ◽  
Precipitin Line ◽  
Tissue Sections ◽  
Immunohistochemical Reaction ◽  
Enzyme Method

Human liver guanase was purified and a specific antibody against it was raised in rabbits. The antiserum formed a single precipitin line with human liver extract, and also completely inhibited the activity of the liver enzyme. An immunoblotting study showed that the antibody bound specifically to one band of protein with guanase activity and not to other proteins. Therefore, we concluded that this antiserum against the liver enzyme was suitable for use in immunohistochemical demonstration of guanase. In tissue sections, the immunohistochemical reaction with this antibody was positive in the same locations as the histochemical guanase reaction with DAB (3,3'-diaminobenzidine tetrahydrochloride).

Lauric acid hydroxylation in human liver and kidney cortex microsomes

1979 ◽  
Vol 28 (23) ◽  
pp. 3385-3390 ◽  
Author(s):  
Richard T. Okita ◽  
Sten W. Jakobsson ◽  
Russell A. Prough ◽  
Bettie Sue Siler Masters
Keyword(s):  
Lauric Acid ◽  
Human Liver ◽  
Kidney Cortex ◽  
Liver And Kidney ◽  
Acid Hydroxylation
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