Chemical cross-linking of membrane-bound rat liver mitochondrial monoamine oxidase

1988 ◽  
Vol 20 ◽  
pp. 77-78
Author(s):  
Anne-Marie O'Carroll ◽  
Keith F. Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Cross Linking ◽  
Mitochondrial Monoamine Oxidase ◽  
Membrane Bound ◽  
Chemical Cross Linking

scholarly journals Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization

1975 ◽  
Vol 145 (2) ◽  
pp. 311-321 ◽  
Author(s):  
M D Houslay ◽  
K F Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Bound State ◽  
Monoamine Oxidase A ◽  
Rate Equations ◽  
British Library ◽  
Ping Pong ◽  
Mitochondrial Monoamine Oxidase ◽  
Lending Library ◽  
Membrane Bound

1. The kinetics of benzylamine oxidation by a soluble preparation of rat liver mitochondrial monoamine oxidase were investigated and were shown to conform to adouble-displacement (or Ping Pong) mechanism. 2. The pathway differs in detail from that followed by other amine oxidases, including the membrane-bound enzyme in rat liver mitochondrial outer membranes. 3. It is suggested taht the conformation of the protein in the soluble state differs from that in the membrane-bound state. 4. The full rate equations for this mechanism have been deposited as Supplementary Publication SUP 50039 (5pages) at the British Library (lending Division) (formely the National Lending Library for Science and Technology), Boston Spa, Yorks, LS237BQ, U.K.. from whom copies can be obtained on the terms indicated in Biochem. J (1975) 145,5.

scholarly journals 5-HYDROXYTRYPTAMINE : A SUBSTRATE FOR RAT LIVER MITOCHONDRIAL MONOAMINE OXIDASE-A AND -B*

1982 ◽  
Vol 32 (5) ◽  
pp. 954-957
Author(s):  
Hiroyasu KINEMUCHI ◽  
Takamori KAWAGUCHI ◽  
Yuichiro ARAI ◽  
Hirohisa TAJIMA ◽  
Lars ORELAND ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Monoamine Oxidase A ◽  
Mitochondrial Monoamine Oxidase

scholarly journals Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg2+-dependent and Ca2+-regulated kinase

2000 ◽  
Vol 352 (1) ◽  
pp. 183-190 ◽  
Author(s):  
Pol HARVENGT ◽  
Ariane VLERICK ◽  
Bruno FUKS ◽  
Ruddy WATTIEZ ◽  
Jean-Marie RUYSSCHAERT ◽  
...  
Keyword(s):  
Stress Responses ◽  
Lens Culinaris ◽  
Kinase Activity ◽  
Cross Linking ◽  
Protein Storage Vacuoles ◽  
Membrane Bound ◽  
Flow Through ◽  
Growth Development ◽  
Chemical Cross Linking ◽  
Aquaporin Family

In plants, aquaporins regulate the water flow through membranes during growth, development and stress responses. We have isolated two isoforms of the aquaporin family from the protein-storage vacuoles of lentil (Lens culinaris Med.) seeds. Chemical cross-linking experiments showed that both isoforms belong to the same oligomer in the membrane and are phosphorylated by a membrane-bound protein kinase. We assigned the kinase activity to a 52kDa protein that is magnesium-dependent and calcium-regulated.

The effect of tris buffers on rat liver mitochondrial monoamine oxidase

1977 ◽  
Vol 29 (1) ◽  
pp. 411-415 ◽  
Author(s):  
C. J. FOWLER ◽  
B. A. CALLINGHAM ◽  
M. D. HOUSLAY
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Mitochondrial Monoamine Oxidase
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