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At least 1,711 records · Page 95Linked to original sources
PubMed1975

Aminopeptidases in webbing clothes moth larvae. Properties and specificities of the enzymes of intermediate electrophoretic mobility.

The major group of aminopeptidases (EC 3.4.11.-) of intermediate electrophoretic mobility, from Tineola bisselliella larvae, hav been fractionated into six bands by preparative polyacrylamide gel electrophoresis and the properties of these fractions investigated. They resemble each other in their pH optima of 8.2, their molecular weight of 240 000, their responses to various active site inhibitors and metal cations, and their specificities towards seventeen L-amino-acyl-beta-naphthylamide substrates. The derivatives of methionine, leucine, alanine, lysine, arginine and glutamic acid were those most rapidly hydrolysed. They appear to be true aminopeptidases hydrolysing amino acid amides, dipeptides and oligopeptides from the N-terminal end.

Amino Acids↗
PubMed1988

Ventricular tachycardia masquerading as supraventricular tachycardia: a wolf in sheep's clothing.

It is generally assumed that if a wide QRS complex tachycardia has the same morphology on the 12-lead electrocardiogram as during sinus rhythm, the tachycardia is supraventricular. The author presents unique electrocardiographic data on four patients with QRS complex morphologies that are nearly identical during ventricular tachycardia and during sinus rhythm. The QRS complex duration during sinus rhythm was 140-180 msec and was the same as that of the tachycardia. The QRS complex morphology on the electrocardiogram was a right bundle branch block, left axis in three patients and right bundle branch block, normal axis in one patient. The mean ventricular tachycardia cycle length was 345 msec. The diagnosis of ventricular tachycardia was established by electrophysiologic testing in two patients and by atrial electrograms demonstrating AV dissociation in two patients. Thus, if the 12-lead electrocardiogram morphology of a wide QRS complex tachycardia is similar to that during sinus rhythm, it does not necessarily imply that the tachycardia is supraventricular. Ventricular tachycardia can occur with the same QRS complex morphology as occurs during sinus rhythm.

Adult↗
PubMed1996

Actinomycosis, a sheep in wolves' clothes.

We present a patient referred for radiotherapy for a presumed pulmonary malignancy, who was found to suffer from an actinomycotic infection. This case illustrates the importance of early consideration of actinomycosis when diagnostic methods are negative for malignancy or specific chestwall and bony lesions are observed.

Actinomycosis↗
PubMed1990

Mentorship--is it a case of the emperors new clothes or a rose by any other name?

The author examines and discusses the concept of mentorship. Consideration is given to the development of mentorship in the United States of America, and to the relevance for adoption in this country. Concern is registered at the absence of a clear definition of the term; its inclusion in course approval criteria and the impact of this is considered. In view of changes in Nurse Education the author questions whether preceptorship might be a more appropriate concept to develop.

Education, Nursing↗
PubMed2005

Heme peroxidase clothing and inhibition with polyphenolic substances revealed by molecular modeling.

Molecular modeling techniques were applied to study oligomeric derivatives of phenols, which are produced during peroxidase-catalyzed oxidation. The interaction of substrates and oligomers with Arthromyces ramosus peroxidase (ARP) was analyzed by docking and molecular dynamics methods. The most possible interaction site of oligomers is the active center of the peroxidase. The affinity of oligomers increases with increasing length of oligomers. However, the complexed oligomers produce non-productive complexes with the peroxidase. Molecular dynamics studies showed that oligomer-peroxidase complexes are stable. It seems likely that strong and stable, but non-productive docking of the oligomers determinates peroxidase inhibition during the reaction by preventing the access of regular substrates to the active center of the enzyme.

Binding Sites↗