Neutralite
Avidin
Neutralite Avidin對BIOTIN具有更高親和力，且更低的背景值。
Recombinant NeutraLite avidin: a non-glycosylated, acidic
mutant of chicken avidin that exhibits high affinity for biotin and low
non-specific binding properties.
Marttila AT,
Laitinen OH,
Airenne KJ,
Kulik T, Bayer EA, Wilchek M, Kulomaa MS.
Source
Department of Biological and Environmental Science,
University of Jyväskylä, 40 351, Jyväskylä, Finland.
Abstract
A recombinant non-glycosylated and acidic form of avidin
was designed and expressed in soluble form in baculovirus-infected insect
cells. The mutations were based on the same principles that guided the design
of the chemically and enzymatically modified avidin derivative, known as
NeutraLite Avidin. In this novel recombinant avidin derivative, five out of the
eight arginine residues were replaced with neutral amino acids, and two of the
lysine residues were replaced by glutamic acid. In addition, the
carbohydrate-bearing asparagine-17 residue was altered to an isoleucine,
according to the known sequences of avidin-related genes. The resultant mutant
protein, termed recombinant NeutraLite Avidin, exhibited superior properties
compared to those of avidin, streptavidin and the conventional NeutraLite
Avidin, prepared by chemo-enzymatic means. In this context, the recombinant
mutant is a single molecular species, which possesses strong biotin-binding
characteristics. Due to its acidic pI, it is relatively free from non-specific
binding to DNA and cells. The recombinant NeutraLite Avidin retains seven
lysines per subunit, which are available for further conjugation and
derivatization.
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