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Immobilization of invertase on sepharose‐linked enzyme glycosyl recognizing polyclonal antibodies
Author(s) -
Jafri Farahdiba,
Saleemuddin M.
Publication year - 1997
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19971220)56:6<605::aid-bit2>3.0.co;2-r
Subject(s) - invertase , polyclonal antibodies , sepharose , glycosyl , enzyme , glycoside hydrolase , chemistry , biochemistry , antibody , chromatography , biology , immunology
Polyclonal antibodies directed against the yeast invertase glycosyls were raised by immunizing rabbits with neoglycoprotein‐I and neoglycoprotein‐II. The neoglycoproteins were prepared by separately coupling the N‐linked large and small molecular weight yeast invertase oligosaccharides respectively to bovine serum albumin with the help of glutaraldehyde. Antibodies specifically recognizing the invertase oligosaccharides were purified from the sera of rabbits immunized with either neoglycoprotein using an affinity column of sepharose 4B‐linked yeast invertase. Specific immunoaffinity supports for the immobilization of invertase were constructed by coupling the affinity‐purified antineoglycoprotein‐I or antineoglycoprotein‐II antibodies to cyanogen bromide activated sepharose‐4B. Both the affinity adsorbants were effective in binding and improving the thermal stability of invertase. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 605–609, 1997.

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