scholarly journals Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from Streptococcus pneumonia serotype 23F

RSC Advances ◽  
2020 ◽  
Vol 10 (50) ◽  
pp. 30110-30114
Author(s):  
Siqiang Li ◽  
Hong Wang ◽  
Guoxia Jin ◽  
Zonggang Chen ◽  
Guofeng Gu
Keyword(s):  
Streptococcus Pneumonia ◽  
Substrate Specificities ◽  
Nucleotide Triphosphates

The broad substrate specificities of thymidylyltransferase Cps23FL towards nucleotide triphosphates and sugar-1-phosphates were systemically investigated.

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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