A comparison of the behavior of chymotrypsin and cathepsin B towards peptidyl diazomethyl ketones.
Explore the source record for details and available documents.
Animals↗
Biomedical subjects
G D Green
Publications and source records attributed to G D Green.
Thiobenzyl benzyloxycarbonyl-L-lysinate, substrate for a sensitive colorimetric assay for trypsin-like enzymes.
Explore the source record for details and available documents.
Colorimetry↗
Failure of pacemaker electrode leads.
With the application of new power sources to pacemakers, considerable improvement has been achieved in the theoretical implant lifetime of current pulse generators, and equally reliable electrode leads will be necessary to ensure long-term pacing. The durability of the electrodes implanted in the past ten years in this centre has been carefully studied. The findings suggest that the use of a more durable conductor material and development of the concept of a 'fail safe' lead (using multi-filament conductors or a secondary conductive pathway along the electrode) will be necessary to match with the implant lifetime of the newer pulse generators. The diagnosis and management of broken conductors is discussed.
Electrodes, Implanted↗
Inactivation of trypsin-like proteases by sulfonylation. Variation of positively charged group and inhibitor length.
Attempts to achieve selective inactivation of serine proteases of closely related specificity (trypsin-like) by aryl sulfonylation have been extended. Nitrophenyl esters of benzenesulfonic acid and phenylmethanesulfonic acid containing various positively charged groups have been synthesized and examined as inactivators of trypsin, thrombin, plasmin, plasma kallikrein, and urokinase. Examples of selective inactivation by isothiouronium derivatives were found and attributed to differences among these enzymes in geometry and flexibility of the primary specificity sites.
Chemical Phenomena↗
Long-term epicardial ventricular pacing from endocardial bipolar pacemaker lead: perforation of right atrial wall.
One of the hazards of endocardial cardiac pacing is that the pacemaker lead may perforate the myocardial wall or interventricular septum although the incidence of such perforations is believed to be small. This paper describes what is believed to be a unique case in which a pacemaker lead perforated the atrial wall at implantation (or possibly shortly afterwards) and yet gave satisfactory right ventricular epicardial pacing for more than five years. The perforation was discovered during a routine postmortem examination but earlier lateral x-ray examinations would probably have identified the abnormal position of the electrodes. Moreover, the present implantation technique would not have allowed perforation of the atrial wall at implantation to go undetected.
Aged↗
Letter: Pacemaker death.
Explore the source record for details and available documents.
Death, Sudden↗
The kinetics of hydrolysis of some extended N-aminoacyl-l-lysine methyl esters.
1. The action of two active forms of bovine trypsin (alpha and beta-trypsin) on a series of specific methyl ester substrates of general formula: N-acetyl-(glycyl)n-L-lysine methyl ester (n = 0, 1, 2) and N2-benzoyl-L-arginine ethyl ester have been investigated. With the L-lysine methyl esters the catalytic rate constant for hydrolysis (kcat) was found to be significantly lower for alpha-trypsin than for beta-trypsin, whereas with N2-benzoyl-L-arginine ethyl ester there was no significant difference for the two enzymes. 2. By measurement of the kinetic constants (kcat and Km) in the presence of a nucleophile, which competes with water in the deacylation process, it has been shown that, in common with the specific ester substrates of trypsin, the rate-determining step for the extended L-lysine methyl esters is decaylation of the enzyme. 3. It has been found that by extending the aminoacyl group of N-acetyl-L-lysine methyl ester by one glycine residue (n = 1), a greatly enhanced deacylation rate constant is observed for both alpha and beta-trypsin. The higher rate constants were maintained at the higher levels by the addition of a further glycine residue (n = 2). These results have been interpreted in terms of the 'induced fit' hypothesis the substrates binding to an enzyme subsite adjacent to the active site. 4. The beta-trypsin-catalysed hydrolysis of the L-lysine substrates was investigated over a range of temperature (15--35 degrees C). The Arrhenius law was obeyed, within experimental error, by all three substrates allowing the estimation of the thermodynamic function of activation (delta S not equal to and deltaH note equal to) for the deacylation reactions. The significantly higher values of deltaS not equal to and deltaH not equal to obtained for the two extended substrates are interpreted in terms of additional hydrogen bonding between the longer aminoacyl chains and the enzyme molecule. The results are compared with those for non-extended specific substrates, which have a possible hydrophobic interaction with the enzyme surface.
Animals↗