A Hin dIII polymorphism at the porcine bone, liver, kidney alkaline phosphatase (ALPL) locus

2009 ◽  
Vol 24 (2) ◽  
pp. 140-140 ◽  
Author(s):  
D. Shalhevet ◽  
D. Krull ◽  
P. Clamp ◽  
R. Feltes ◽  
E. Atac ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
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.

A kinetic study of rat kidney alkaline phosphatase

1967 ◽  
Vol 122 (2) ◽  
pp. 417-420 ◽  
Author(s):  
F. Melani ◽  
M. Farnararo ◽  
G. Sgaragli
Keyword(s):  
Alkaline Phosphatase ◽  
Kinetic Study ◽  
Rat Kidney ◽  
Kidney Alkaline Phosphatase

Phosphatases. II. Changes in the composition of human intestinal and kidney alkaline phosphatase during purification

1965 ◽  
Vol 30 (11) ◽  
pp. 3964-3968 ◽  
Author(s):  
B. Večerek ◽  
J. Kraml ◽  
H. Pelichová ◽  
J. Štěpán ◽  
M. Chmelař ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Kidney Alkaline Phosphatase

scholarly journals The reversible inactivation of pig kidney alkaline phosphatase at low pH

1968 ◽  
Vol 108 (2) ◽  
pp. 243-246 ◽  
Author(s):  
P. J. Butterworth
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Treatment ◽  
Gel Filtration ◽  
Reversible Inactivation ◽  
Pig Kidney ◽  
Reactivation Mechanism ◽  
Increasing Temperature ◽  
Filtration Properties ◽  
Kinetics Of ◽  
Kidney Alkaline Phosphatase

1. Pig kidney alkaline phosphatase is inactivated by treatment with acid at 0°. 2. Inactivated enzyme can be partially reactivated by incubation at 30° in neutral or alkaline buffer. The amount of reactivation that occurs depends on the degree of acid treatment; enzyme that has been inactivated below pH3·3 shows very little reactivation. 3. Studies of the kinetics of reactivation indicate that the process is greatly accelerated by increasing temperature and proceeds by a unimolecular mechanism. The reactivated enzyme has electrophoretic and gel-filtration properties identical with those of non-treated enzyme. 4. The results can be best explained by assuming that a lowering of the pH causes a reversible conformational change of the alkaline phosphatase molecule to a form that is no longer enzymically active but is very susceptible to permanent denaturation by prolonged acid treatment. A reactivation mechanism involving sub-unit recombination seems unlikely.

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