The Major Soybean Allergen Gly m Bd 28K Induces Hypersensitivity Reactions in Mice Sensitized to Cow's Milk Proteins [PDF]
Reactions to soy have been reported in a proportion of patients with IgE-mediated cow’s milk allergy (CMA). In this work, we analyzed if Gly m Bd 28K/P28, one of the major soybean allergens, is a cross-reactive allergen with cow milk proteins (CMP).
Candreva, Ángela María+5 more
core +2 more sources
Maltose-binding protein is a periplasmic binding protein responsible for transport of maltooligosaccarides through the periplasmic space of Gram-negative bacteria, as a part of the ABC transport system.
Wenjuan Huang+3 more
semanticscholar +1 more source
Location of tolerated insertions/deletions in the structure of the maltose binding protein [PDF]
In a previous study [(1987) J. Mol. Biol. 194, 663‐673], we isolated ten insertion/deletion mutants (indels) of the maltose binding protein for which the maltose binding constant was only a little or not at all affected. In this paper, we have localized these mutations in the recently solved three‐dimensional structure.
Maurice Hofnung+3 more
openaire +3 more sources
Mutations in maltose-binding protein that alter affinity and solubility properties [PDF]
Maltose-binding protein (MBP) from Escherichia coli has been shown to be a good substrate for protein engineering leading to altered binding (Marvin and Hellinga, Proc Natl Acad Sci U S A 98:4955-4960, 2001a) and increased affinity (Marvin and Hellinga, Nat Struct Biol 8:795-798, 2001b; Telmer and Shilton, J Biol Chem 278:34555-34567, 2003). It is also
Pei-Chung Hsieh+2 more
openaire +3 more sources
A full-length cDNA encoding a candidate Oxysterol-binding protein(OSBP) from Aspergillus oryzae (AoOSBP) was cloned and expressed in Escherichia coli as a maltose-binding protein (MBP) fusion protein.
Zhang Xian+4 more
doaj +1 more source
Expression and Purification of the Arabidopsis E4 SUMO Ligases PIAL1 and PIAL2
The proteins PIAL1 (At1g08910) and PIAL2 (At5g41580) are members of the recently discovered group of plant E4 SUMO ligases. This protocol allows quick and simple expression of the recombinant proteins in Escherichia coli (E.
Konstantin Tomanov, Andreas Bachmair
doaj +1 more source
Virtual Identification of Essential Proteins Within the Protein Interaction Network of Yeast [PDF]
Topological analysis of large scale protein-protein interaction networks (PINs) is important for understanding the organisational and functional principles of individual proteins. The number of interactions that a protein has in a PIN has been observed to be correlated with its indispensability.
arxiv +1 more source
The Binding of Maltose to ‘Virgin’ Maltose‐Binding Protein is Biphasic [PDF]
The biphasic binding properties of the galactose‐binding and maltose‐binding proteins of Escherichia coli may be important in the functioning of these proteins as recognition components of chemoreceptors. However, Richarme and Kepes [Eur. J. Biochem. 45, 127‐133 (1974)] have suggested that the biphasic binding curve of the galactose‐binding protein may
openaire +3 more sources
Stimulation of the Maltose Transporter ATPase by Unliganded Maltose Binding Protein [PDF]
ATP hydrolysis by the maltose transporter (MalFGK(2)) is regulated by maltose binding protein (MBP). Binding of maltose to MBP brings about a conformational change from open to closed that leads to a strong stimulation of the MalFGK(2) ATPase. In this study, we address the long-standing but enigmatic observation that unliganded MBP is also able to ...
Gould, Alister D.+2 more
openaire +5 more sources
Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
We describe a rapid, simple, and efficient method for recovering glutathione S-transferase (GST)- and His6-tagged maltose binding protein (MBP) fusion proteins from inclusion bodies.
Hu Tao+5 more
doaj +1 more source