A new micromethod for mechano-chemical research.
A new micromethod to study activity of enzymes in crystalline and amorphous solid samples subjected to tension is described. Both static (up to 200%) and dynamic (with an amplitude up to 50% and frequency of 10(-3)-50 Hz) deformation may be applied to the sample during the activity measurement. Strain-induced changes in activity of thin (3-10 microns) needle-like strips (0.2-0.5 microns long), cut out of the microtome sections of cross-linked crystals of pancreatic carboxypeptidase A is measured in a droplet of substrate solution (with volume of 10(-6)-10(-9) l) with a pH-microelectrode technique.
Morozov
V N
VN
Institute of Theoretical and Experimental Biophysics, Academy of Sciences of the USSR, Pushchino, Moscow Region.
Gorelov
A V
AV
Zenchenko
T A
TA
D002268:Carboxypeptidases / Q000737:chemistry; D043422:Carboxypeptidases A; D002627:Chemistry, Physical / Q000295:instrumentation / Q000379:methods*; D003432:Cross-Linking Reagents / Q000737:chemistry; D003460:Crystallization; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008832:Microchemistry / Q000295:instrumentation / Q000379:methods*; D013314:Stress, Mechanical
D003432:Cross-Linking Reagents; D004798:Enzymes; D002268:Carboxypeptidases; D043422:Carboxypeptidases A