๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Comparison of a new amylase found in barley with the amylases of the fungi of barley husk

โœ Scribed by Marja-Leena Niku-Paavola; Marjatta Heikkinen


Publisher
John Wiley and Sons
Year
1975
Tongue
English
Weight
227 KB
Volume
26
Category
Article
ISSN
0022-5142

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Further purification and characterisatio
โœ Alexander W. Macgregor; Jean Daussant; Marja-L Niku-Paavola ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 406 KB

## Abstract An amylase, previously detected in barley and described as a new barley amylase, has been further purified by immunoโ€affinity and ion exchange chromatography on CMโ€cellulose Analysis by isoelectricfocusing and immunochemical techniques showed that thses enzyme preparation did not contai

Amylose chain behavior in an interacting
โœ G. Andrรฉ; A. Bulรฉon; R. Haser; V. Tran ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 107 KB ๐Ÿ‘ 2 views

In the first two papers of this series, the tools necessary to evaluate substrate ring deformations were developed, and then the modeling of short amylose fragments (maltotriose and maltopentaose) inside the catalytic site of barley alpha-amylase was performed. In this third paper, this docking has

Amylose chain behavior in an interacting
โœ G. Andrรฉ; A. Bulรฉon; M. Juy; N. Aghajari; R. Haser; V. Tran ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 131 KB ๐Ÿ‘ 2 views

In the first paper of this series, the tools necessary to evaluate the consequences of glucopyranose ring deformations in terms of glycosidic torsion angle shifts, and amylose chain propagation have been created. In this second paper, the modeling of amylose fragments into the catalytic region of ba

Solution conformation of an immunogenic
โœ M. Antรฒnia Molins; Miquel ร€ngel Contreras; Ignacio Fita; Miquel Pons ๐Ÿ“‚ Article ๐Ÿ“… 1998 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 175 KB ๐Ÿ‘ 2 views

The conformation of a [15]-peptide (H-VKAETRLNPDLQPTE-NH 2 ) from VP2 of rhinovirus HRV2 complexed with a Fab fragment was previously shown by X-ray crystallographic studies to be similar to the one found in the corresponding region of HRV1A. Antibodies raised against this peptide bind to and neutra