M. Brenner

Bio: M. Brenner is an academic researcher from University of Basel. The author has contributed to research in topics: Thin-layer chromatography & Hydroxylamine. The author has an hindex of 17, co-authored 52 publications receiving 1612 citations.

Herstellung von α‐Aminosäureestern durch Alkoholyse der Methylester

Abstract: Die Alkoholyse von α-Aminosauremethylestern ist zur Gewinnung von Aminosaureestern schwerfluchtiger Alkohole brauchbar. Bei Verwendung von Natriumalkoxyd als Umesterungskatalysator erfolgt am α-Kohlenstoffatom der Aminosaure ganz oder teilweise Racemisierung; die optische Aktivitat bleibt dagegen erhalten, wenn als Katalysator ein Aluminiumalkoxyd verwendet wird. Die benotigten Aminosaure-methylester konnen, namentlich wenn sie in grosseren Mengen gebraucht werden, auf einfachste Weise mit Hilfe von Thionylchlorid hergestellt werden.

Amino Acids and Derivatives

Abstract: Free amino acids and peptides are markedly hydrophilic compounds, only slightly soluble in non-aqueous solvents. This must be borne in mind when sampling and preparing materials for TLC as well as when choosing the solvent. Some data on solubilities of a few amino acids in various solvents which illustrate this are:

Dünnschicht-Chromatographie von Aminosäuren auf Kieselgel G. 2. Mitteilung. Eine Schnellmethode zur Trennung und zum qualitativen Nachweis von 22 Aminosäuren

Abstract: A thin layer chromatographic methods for rapid separation and detection of 22 commonly occurring amino-acids is described. Special reference is made to the analysis of protein hydrolysates and to the sensitivity of the ninhydrin reaction.

Eine neue enzymatische Peptidsynthese. 1. Mitteilung

Abstract: Die Ester des Methionins und einiger anderer spezifischer Aminosauren reagieren in Gegenwart von Wasser und kauflichen Praparaten von kristallisiertem Chymotrypsin unter Bildung von Peptiden.

Thin-layer chromatography of lipids

Abstract: Technique Thin-Layer Chromatography as an Analytical Tool Qualitative Analysis Quantitative Analysis Thin-Layer Chromatography as a Preparative Tool

Enzymes that degrade bacterial cell walls

Abstract: Publisher Summary This chapter focuses on the mechanism of enzymes that degrade bacterial cell walls. The cell walls of all bacteria are composed of two or more polymers. They are ubiquituous in the bacterial world, are responsible for the shape and strength of the walls, and allow the cells to live in environmental conditions which are hypotonic with respect to their high intracellular osmotic pressure. These polymers are a glycopeptide built up of polyacetylhexosamine and peptide chains, and the action of all bacteriolytic enzymes. The basic structure of the peptide subunits is probably similar to that found in uridine diphosphate (UDP)-acetylmuramyl-peptide cell wall precursors. Some or all of the peptide chains linked to adjacent polysaccharide backbones are in turn linked to each other, resulting in a network of at least two dimensions. The digestion of different bacterial walls by various bacteriolytic enzymes gives rise to fragments of highly diverse nature and molecular complexity. A lyric intrapeptide hydrolase induces the appearance of new terminal amino and carboxyl groups. The enzymes that degrade the glycopeptide of bacterial cell walls and of which the specificity is at least partially known, are tabulated in the chapter.

Solid-phase peptide synthesis.

Abstract: It is a privilege to be able to contribute to this volume in which Professor Zervas’ friends, students, and colleagues have joined together to honor him and his remarkable contributions to peptide chemistry. Although I did not know him until after his days in the Bergmann Laboratory at the Rockefeller Institute, I can claim the distinction of now working in those very same rooms that they occupied back in the mid-1930s. Like all peptide chemists, I am greatly indebted to Professor Zervas, having depended so heavily on the carbobenzoxy group and on the various modified urethan protecting groups which have been direct extensions of the revolutionary advance that Bergmann and Zervas made.