scholarly journals Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue

1985 ◽  
Vol 227 (3) ◽  
pp. 1031-1031
Keyword(s):  
Substrate Specificities ◽  
Oleate Desaturase ◽  
Desaturase System

scholarly journals Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue

1985 ◽  
Vol 225 (1) ◽  
pp. 267-270 ◽  
Author(s):  
D J Murphy ◽  
I E Woodrow ◽  
K D Mukherjee
Keyword(s):  
Pisum Sativum ◽  
Microsomal Fraction ◽  
Major Product ◽  
Acyl Transfer ◽  
Functional Coupling ◽  
Substrate Specificities ◽  
Oleate Desaturase ◽  
Pisum Sativum L ◽  
Bulk Membrane ◽  
Desaturase System

In the microsomal fraction from young pea (Pisum sativum L.) leaves, the oleoyl moieties from oleoyl-CoA are principally transferred to the sn-2 position of phosphatidylcholine by oleoyl-CoA:1-acyl-lysophosphatidylcholine acyltransferase. The major product of this acyl transfer is 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine. The 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine is subsequently converted into 1-palmitoyl(stearoyl)-2-linoleoyl phosphatidylcholine by the oleate desaturase complex without equilibrating with the bulk membrane phosphatidylcholine pool. Hence, both the acyl transfer to phosphatidylcholine and the subsequent desaturation of oleoyl moieties occur on the sn-2 position of phosphatidylcholine, and there is also a functional coupling of the acyltransferase and oleate desaturase.

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 A comparison of the substrate specificities of cathepsin D and pseudorenin.

1978 ◽  
Vol 253 (9) ◽  
pp. 3140-3142 ◽  
Author(s):  
F.E. Dorer ◽  
K.E. Lentz ◽  
J.R. Kahn ◽  
M. Levine ◽  
L.T. Skeggs
Keyword(s):  
Cathepsin D ◽  
Substrate Specificities

scholarly journals Substrate specificities of tyrosine-specific protein kinases toward cytoskeletal proteins in vitro.

1986 ◽  
Vol 261 (31) ◽  
pp. 14797-14803 ◽  
Author(s):  
T Akiyama ◽  
T Kadowaki ◽  
E Nishida ◽  
T Kadooka ◽  
H Ogawara ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Specific Protein ◽  
Cytoskeletal Proteins ◽  
Substrate Specificities

scholarly journals Different substrate specificities of the two DNA ligases of mammalian cells.

1986 ◽  
Vol 261 (20) ◽  
pp. 9079-9082 ◽  
Author(s):  
J E Arrand ◽  
A E Willis ◽  
I Goldsmith ◽  
T Lindahl
Keyword(s):  
Mammalian Cells ◽  
Substrate Specificities ◽  
Dna Ligases
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