✦ LIBER ✦

Modification of food proteins by covalent crosslinking

✍ Scribed by Harjinder Singh

Book ID: 118008514
Publisher: Elsevier Science
Year: 1991
Tongue: English
Weight: 525 KB
Volume: 2
Category: Article
ISSN: 0924-2244
DOI: 10.1016/0924-2244(91)90683-a

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Regulation of G proteins by covalent mod

Regulation of G proteins by covalent modification

✍ Chen, Catherine A; Manning, David R 📂 Article 📅 2001 🏛 Nature Publishing Group 🌐 English ⚖ 177 KB

Crosslinking Between Different Food Prot

Crosslinking Between Different Food Proteins by Transglutaminase

✍ MASAO MOTOKI; NORIKI NIO 📂 Article 📅 1983 🏛 Institute of Food Technologists 🌐 English ⚖ 710 KB

Surface modification of proteins by cova

Surface modification of proteins by covalent binding of acrylic polymers

✍ Francesco M. Veronese; Roberta Largajolli; Carlo Visco; Paolo Ferruti; Adelaide 📂 Article 📅 1985 🏛 Springer-Verlag 🌐 English ⚖ 460 KB

Covalent vectored binding of functional

Covalent vectored binding of functional proteins by bifunctional crosslinking at silicone interfaces

✍ Andreas Steiert; Kerstin Reimers; William Burke; Antonia Zapf; Peter Vogt 📂 Article 📅 2012 🏛 John Wiley and Sons 🌐 English ⚖ 912 KB

Covalent Protein Crosslinks: General Det

Covalent Protein Crosslinks: General Detection, Quantitation, and Characterization via Modification with Diphenylborinic Acid

✍ L. Graham; P.M. Gallop 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 670 KB

Progressive crosslinking of proteins appears to be a general phenomenon in aging cells and tissues. Crosslinked proteins can form insoluble aggregates which become increasingly resistant to proteolysis as more crosslinks form. However, most evidence for progressive crosslinking with age is indirect,

Chemical modification of crayfish axons

Chemical modification of crayfish axons by protein crosslinking aldehydes

✍ Peter G. Shrager; Alfred Strickholm; Robert I. Macey 📂 Article 📅 1969 🏛 John Wiley and Sons 🌐 English ⚖ 725 KB

A series of aldehydes of varying protein crosslinking strengths have been tested on intact and internally perfused crayfish axons. Non-crosslinking aldehydes have no effect, or cause a gradual decline in resting potential and overshoot with no widening of the spike. Strong crosslinking compounds, su