Long-Term Dynamic of Anti-TrimericS and Anti-RBD Antibodies in Naive and COVID-19 Recovered mRNA-1273 Vaccine Recipients.

Objective: Patients and physicians are increasingly requesting their clinical laboratory to provide SARS-CoV-2 serology interpretation. Our study aimed to assess the evolution of SARS-CoV-2 antibodies in Moderna-vaccinated health care workers.

Methods: We analyzed the evolution of mRNA-1273 (Moderna)-elicited antibodies by 2 high-throughput assays, TrimericS IgG (Diasorin) and SARS-CoV-2 IgG-II (Abbott).

Development of a sub-hour on-line comprehensive cation exchange chromatography x RPLC method hyphenated to HRMS for the characterization of lysine-linked antibody-drug conjugates.

This study details the development of on-line two-dimensional liquid chromatography (2D-LC) methods combining cation-exchange chromatography (CEX) and reversed-phase liquid chromatography (RPLC) for the separation of the charge variants of a lysine-linked antibody-drug conjugate (ADC). This combination gives an excellent example of the potential benefits of 2D-LC approaches for the analysis of such complex protein formats. CEX is considered the reference technique for the separation of protein charge variants but its retention mechanism usually requires the use of a high concentration of non-volatile salts, which impedes its compatibility with MS detection.

Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study.

We previously showed that one-electron transfer from tetrahydropterins to iron porphyrins is a very general reaction, with formation of an intermediate cation radical similar to the one detected in NO synthase. As a model reaction, the rates of reduction of eight haemoproteins by diMePH4 (6,7-dimethyltetrahydropterin) have been studied and correlated with their one-electron reduction potentials, E(m) (Fe(III)/Fe(II)). On the basis of kinetic data analyses, a bimolecular collisional mechanism is proposed for the electron transfer from diMePH4 to ferrihaemoproteins.

Very general formation of tetrahydropterin cation radicals during reaction of iron porphyrins with tetrahydropterins: model for the corresponding NO-synthase reaction.

Electron transfer from tetrahydropterins to iron porphyrins, with formation of intermediate tetrahydropterin cation radicals, is a very general reaction that was shown to occur not only with tetrahydrobiopterin, as originally found in NO-synthases, but also with another important biological cofactor, tetrahydrofolate, and various iron porphyrins, either in their ferric state, or in the Fe(II)O(2) state, as in the first model of the corresponding NO-synthase reaction described in this paper.