scholarly journals Bovine kidney alkaline phosphatase. Catalytic properties, subunit interactions in the catalytic process, and mechanism of Mg2+ stimulation.

1975 ◽  
Vol 250 (15) ◽  
pp. 6046-6053 ◽  
Author(s):  
G Cathala ◽  
C Brunel
Keyword(s):  
Alkaline Phosphatase ◽  
Catalytic Properties ◽  
Catalytic Process ◽  
Subunit Interactions ◽  
Bovine Kidney ◽  
Kidney Alkaline Phosphatase

Multiple forms of bovine kidney alkaline phosphatase

1981 ◽  
Vol 14 (3) ◽  
pp. 150-152 ◽  
Author(s):  
Kevin Cavanagh ◽  
K. Kithier ◽  
R.J. Thibert ◽  
H.F. Fackrell
Keyword(s):  
Alkaline Phosphatase ◽  
Multiple Forms ◽  
Bovine Kidney ◽  
Kidney Alkaline Phosphatase

Cloning and sequencing of bovine kidney alkaline phosphatase cDNA

Gene ◽  
1987 ◽  
Vol 59 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Enrico Garattini ◽  
Jia Cheng Hua ◽  
Sidney Udenfriend
Keyword(s):  
Alkaline Phosphatase ◽  
Cloning And Sequencing ◽  
Bovine Kidney ◽  
Kidney Alkaline Phosphatase

Purification and partial amino acid sequencing of bovine kidney alkaline phosphatase

1987 ◽  
Vol 19 (5) ◽  
pp. 413-417 ◽  
Author(s):  
Howard H.T. Hsu ◽  
Jim Rouse ◽  
James Hamilton ◽  
H.Clarke Anderson
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequencing ◽  
Bovine Kidney ◽  
Kidney Alkaline Phosphatase

scholarly journals Evidence for the importance of arginine residues in pig kidney alkaline phosphatase

1979 ◽  
Vol 181 (1) ◽  
pp. 137-142 ◽  
Author(s):  
M N Woodroofe ◽  
P J Butterworth
Keyword(s):  
Alkaline Phosphatase ◽  
Active Site ◽  
Competitive Inhibitor ◽  
Arginine Residue ◽  
Pig Kidney ◽  
Close Proximity ◽  
Arginine Residues ◽  
Km Value ◽  
Uncompetitive Inhibitor ◽  
Kidney Alkaline Phosphatase

The arginine-specific reagents 2,3-butanedione and phenylglyoxal inactivate pig kidney alkaline phosphatase. As inactivation proceeds there is a progressive fall in Vmax. of the enzyme, but no demonstrable change in the Km value for substrate. Pi, a competitive inhibitor, and AMP, a substrate of the enzyme, protect alkaline phosphatase against the arginine-specific reagents. These effects are explicable by the assumption that the enzyme contains an essential arginine residue at the active site. Protection is also afforded by the uncompetitive inhibitor NADH through a partially competive action against the reagents. Enzyme that has been exposed to the reagents has a decreased sensitivity to NADH inhibition. It is suggested that an arginine residue is important for NADH binding also, although this residue is distinct from that at the catalytic site. The protection given by NADH against loss of activity is indicative of the close proximity of the active and NADH sites.

Identification of Functional Groups of Pig Kidney Alkaline Phosphatase by Specific Inhibitors

1975 ◽  
Vol 30 (11-12) ◽  
pp. 829-831 ◽  
Author(s):  
Jan Ahlers
Keyword(s):  
Alkaline Phosphatase ◽  
Functional Groups ◽  
Pig Kidney ◽  
Kidney Alkaline Phosphatase ◽  
Specific Inhibitors ◽  
Regulatory Sites

Abstract Inactivation studies with 17 group-specific inhibitors showed that amino, hystidyl and tyrosyl residues probably are components of the active and/or regulatory sites of pig kidney alkaline phosphatase.

Alkaline Phosphatase from Rabbit Kidney: Studies on the Catalytic Properties of Its Multiforms

1977 ◽  
Vol 81 (6) ◽  
pp. 1813-1823 ◽  
Author(s):  
C.S. RAMADOSS ◽  
R. SELVAM ◽  
K Radha SHANMUGASUNDARAM ◽  
E.R.B. SHANMUGASUNDARAM
Keyword(s):  
Alkaline Phosphatase ◽  
Catalytic Properties ◽  
Rabbit Kidney
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