SOME PROPERTIES OF AN ALKALINE PHOSPHATASE FROM RAT ADIPOSE TISSUE

1964 ◽  
Vol 42 (10) ◽  
pp. 1445-1457 ◽  
Author(s):  
Donald P. Wallach ◽  
Howard Ko
Keyword(s):  
Alkaline Phosphatase ◽  
Adipose Tissue ◽  
Kinetic Data ◽  
Aqueous Extracts ◽  
Partial Inhibition ◽  
Metallic Cation ◽  
Inhibition Kinetic ◽  
Salient Features ◽  
Rat Adipose Tissue ◽  
Ethylene Diaminetetraacetic Acid

An alkaline phosphatase was partially purified from aqueous extracts of rat adipose tissue, and some characteristics of the enzyme delineated. Among salient features, the enzyme is strongly inhibited by cysteine and ethylene diaminetetraacetic acid (EDTA) and types of inhibition were determined. Cysteine induced "complete exclusive" inhibition, while EDTA caused "partial" inhibition. Kinetic data on the inhibition by EDTA are consistent with a mechanism which does not involve chelation of a metallic cation. Various other properties of the enzyme are discussed.

scholarly journals Rat adipose-tissue glycerol phosphate acyltransferase can be inactivated by cyclic AMP-dependent protein kinase

1978 ◽  
Vol 176 (2) ◽  
pp. 607-610 ◽  
Author(s):  
H G Nimmo ◽  
B Houston
Keyword(s):  
Alkaline Phosphatase ◽  
Adipose Tissue ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Hormonal Control ◽  
Glycerol Phosphate ◽  
Dependent Protein Kinase ◽  
Phosphorylation Reaction ◽  
Dependent Protein ◽  
Rat Adipose Tissue

Rat adipose-tissue glycerol phosphate acyltransferase can be inactivated in a phosphorylation reaction catalysed by cyclic AMP-dependent protein kinase and reactivated by treatment with alkaline phosphatase. These results suggest that phosphorylation of glycerol phosphate acyltransferase may be involved in the hormonal control of esterification.

Simultaneous Determinations of Liver- and Bone-Type Alkaline Phosphatase by Curve-Fitting of Inhibition Kinetic Data. II. Development and Evaluation of a Fluorescence-Based Method

1992 ◽  
Vol 38 (2) ◽  
pp. 247-255 ◽  
Author(s):  
Carol P Fitzpatrick ◽  
Harry L Pardue
Keyword(s):  
Alkaline Phosphatase ◽  
Kinetic Data ◽  
Kinetic Method ◽  
Linear Least Squares ◽  
First Order ◽  
Least Squares Fit ◽  
Inhibition Kinetic ◽  
Substrate Concentrations ◽  
Measurement Period

Abstract We describe a kinetic method for the determination of alkaline phosphatase (ALP) isoenzymes, based on fluorescence detection of 4-methylumbelliferone. Several different buffer-inhibitor combinations and substrate concentrations were evaluated. Best results were obtained for inhibition with 2.9 mol/L urea in amino-2-methyl-1-propanol buffer. With this combination, normal concentrations of bone- and liver-type ALP could be determined from kinetic data during an 8-min measurement period. We computed initial velocities from parameters for first-order fits during 1.2 half-lives of the response for liver-type ALP. A linear least-squares fit of initial velocities (y) determined in this way vs results obtained with a comparison procedure (x) gave good correlations. We also estimated total signal changes, delta S, from first-order fits during four half-lives. Isoenzyme content correlated well with parameters computed from the first-order fits. Values for standard errors of the estimates represent 5% and 3% of median responses for activities and isoenzyme content, respectively. When compared with an absorbance-based method described previously, this method had threefold shorter measurement times, but imprecisions were 1.6- to 1.8-fold larger.

scholarly journals Effects of age and cell size on rat adipose tissue metabolism.

1975 ◽  
Vol 16 (6) ◽  
pp. 461-464 ◽  
Author(s):  
G Holm ◽  
B Jacobsson ◽  
P Björntorp ◽  
U Smith
Keyword(s):  
Adipose Tissue ◽  
Cell Size ◽  
Adipose Tissue Metabolism ◽  
Tissue Metabolism ◽  
Rat Adipose Tissue
Sign in / Sign up

Export Citation Format

Share Document