.alpha.-Amino aldehyde equivalents as substrates for rabbit muscle aldolase: synthesis of 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis(hydroxymethyl)-3(R),4(R)-dihydroxypyrrolidine

1991 ◽  
Vol 56 (12) ◽  
pp. 3849-3855 ◽  
Author(s):  
Rebecca R. Hung ◽  
Julie Ann Straub ◽  
George M. Whitesides
Keyword(s):  
Rabbit Muscle ◽  
Amino Aldehyde

Destruction of Actin Filaments by Osmium Tetroxide

1977 ◽  
Vol 35 ◽  
pp. 466-467
Author(s):  
P. Maupin-Szamier ◽  
T. D. Pollard
Keyword(s):  
Actin Filaments ◽  
Time Course ◽  
Osmium Tetroxide ◽  
Rabbit Muscle ◽  
Muscle Actin ◽  
Sodium Phosphate Buffer ◽  
Transmission Electron ◽  
The Difference ◽  
Rates Of Decay ◽  
Short Time

We have studied the destruction of rabbit muscle actin filaments by osmium tetroxide (OSO4) to develop methods which will preserve the structure of actin filaments during preparation for transmission electron microscopy.Negatively stained F-actin, which appears as smooth, gently curved filaments in control samples (Fig. 1a), acquire an angular, distorted profile and break into progressively shorter pieces after exposure to OSO4 (Fig. 1b,c). We followed the time course of the reaction with viscometry since it is a simple, quantitative method to assess filament integrity. The difference in rates of decay in viscosity of polymerized actin solutions after the addition of four concentrations of OSO4 is illustrated in Fig. 2. Viscometry indicated that the rate of actin filament destruction is also dependent upon temperature, buffer type, buffer concentration, and pH, and requires the continued presence of OSO4. The conditions most favorable to filament preservation are fixation in a low concentration of OSO4 for a short time at 0°C in 100mM sodium phosphate buffer, pH 6.0.

P1, P5-Bis-(5′-adenosyl)pentaphosphate: Is this Adenylate Kinase Inhibitor Substrate for Mitochondrial Processes?

1977 ◽  
Vol 32 (9-10) ◽  
pp. 786-791 ◽  
Author(s):  
Josef Köhrle ◽  
Joachim Lüstorff ◽  
Eckhard Schlimme
Keyword(s):  
Adenylate Kinase ◽  
Kinase Inhibitor ◽  
Adenine Nucleotide ◽  
Nucleoside Diphosphate Kinase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Intermembrane Space ◽  
Rabbit Muscle ◽  
Inner Mitochondrial Membrane

Abstract 1. P1, P5-Bis-(5′-adenosyl)pentaphosphate (Ap5A) inhibits “soluble” adenylate kinase even when this enzyme is an integral part of the complete mitochondrion. The Ki is 10-5м , i. e. about two orders of magnitude higher than the inhibitor constants determined for the purified adenylate kinase of rabbit muscle and an enzyme preparation separated from the mitochondrial intermembrane space. The weaker inhibitory effect is due to a lower accessibility of the enzyme.2. As to be expected Ap5A which is of the “multisubstrate analogue”-type does not affect mito­ chondrial nucleoside diphosphate kinase.3. Though Ap5A owns the structural elements of both ATP and ADP it is not a substrate of the adenine nucleotide carrier, i.e. neither it is exchanged across the inner mitochondrial membrane nor specifically bound.4. Ap5A is not metabolized by rat liver mitochondria.

scholarly journals Mechanism of Action of Rabbit Muscle Phosphoglucomutase

1974 ◽  
Vol 249 (10) ◽  
pp. 3166-3169 ◽  
Author(s):  
Olov Wålinder ◽  
Jayant G. Joshi
Keyword(s):  
Mechanism Of Action ◽  
Rabbit Muscle

scholarly journals Pseudoisoenzymes of Rabbit Muscle Phosphoglucose Isomerase

1972 ◽  
Vol 247 (4) ◽  
pp. 1170-1179
Author(s):  
Michael N. Blackburn ◽  
John M. Chirgwin ◽  
Gordon T. James ◽  
Thomas D. Kempe ◽  
Thomas F. Parsons ◽  
...  
Keyword(s):  
Phosphoglucose Isomerase ◽  
Rabbit Muscle
Sign in / Sign up

Export Citation Format

Share Document