Exploring ultrasound and electromyography for carpal tunnel syndrome diagnosis: a comprehensive comparative study and implications for occupational medicine.

Background: To assess the contribution of ultrasound in diagnosing occupational carpal tunnel syndrome (CTS), compare it with electromyography (EMG) results, and evaluate the ultrasound characteristics of CTS patients.

Methods: A nine-month cross-sectional study (January-September 2021) involved CTS patients and a control group, utilizing a structured form for data collection. EMG was performed on the patient group ('cases') and ultrasound examinations were conducted on both groups.

Effect of Tris Buffer in the Intensity of the Multipoint Covalent Immobilization of Enzymes in Glyoxyl-Agarose Beads.

Tris is an extensively used buffer that presents a primary amine group on its structure. In the present work trypsin, chymotrypsin and penicillin G acylase (PGA) were immobilized/stabilized on glyoxyl agarose in presence of different concentrations of Tris (from 0 to 20 mM). The effects of the presence of Tris during immobilization were studied analyzing the thermal stability of the obtained immobilized biocatalysts.

Effect of Concentrated Salts Solutions on the Stability of Immobilized Enzymes: Influence of Inactivation Conditions and Immobilization Protocol.

This paper aims to investigate the effects of some salts (NaCl, (NH)SO and NaSO) at pH 5.0, 7.0 and 9.

Effect of amine length in the interference of the multipoint covalent immobilization of enzymes on glyoxyl agarose beads.

Trypsin, chymotrypsin, penicillin G acylase and ficin extract have been stabilized by immobilization on glyoxyl agarose, adding different aliphatic compounds bearing a primary amine group during the immobilization: ethyl amine, butyl amine, hexyl amine (at concentrations ranging from 0 to 20 mM) and octyl amine (from 0 to 10 mM) to analyze their effects on the immobilized enzyme stability. As expected, the presence of amines reduced the intensity of the enzyme-support multipoint covalent attachment, and therefore the enzyme stability. However, it is clear that this effect is higher using octyl amine for all enzymes (in some cases the enzyme immobilized in the presence of 10 mM octyl amine was almost inactivated while the reference kept over 50 % of the initial activity).