In vitro galactosylation of rhodopsin and opsin: Kinetics, properties and characterization

Ju, Jr-Min; Kean, Edward L.

doi:10.1016/s0014-4835(05)80172-1

Cited by 8 publications

(1 citation statement)

References 49 publications

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“…The product of the three-step synthesis is a protein-bound form of sialyl Lewis x. Other examples can be found in Ju and Kean [124] and Schneider et al [125].…”

Section: A-26-sialyltransferasesmentioning

confidence: 99%

Untitled

Malissard

Zeng

Berger

1999

Glycoconjugate Journal

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Glycosyltransferases are increasingly being used for in vitro synthesis of oligosaccharides. Since these enzymes are difficult to purify from natural sources, expression systems for soluble forms of the recombinant enzymes have been developed. This review focuses on the current state of development of yeast expression systems. Two yeast species have mainly been used, i.e. Saccharomyces cerevisiae and Pichia pastoris. Safety and ease of fermentation are well recognized for S. cerevisiae as a biotechnological expression system; however, even soluble forms of recombinant glycosyltransferases are not secreted. In some cases, hyperglycosylation may occur. P. pastoris, by contrast, secrete soluble orthoglycosylated forms to the supernatant where they can be recovered in a highly purified form. The review also covers some basic features of yeast fermentation and describes in some detail those glycosyltransferases that have successfully been expressed in yeasts. These include beta1,4galactosyltransferase, alpha2,6sialyltransferase, alpha2,3sialyltransferase, alpha1,3fucosyltransferase III and VI and alpha1,2mannosyltransferase. Current efforts in introducing glycosylation systems of higher eukaryotes into yeasts are briefly addressed.

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“…The product of the three-step synthesis is a protein-bound form of sialyl Lewis x. Other examples can be found in Ju and Kean [124] and Schneider et al [125].…”

Section: A-26-sialyltransferasesmentioning

confidence: 99%

Untitled

Malissard

Zeng

Berger

1999

Glycoconjugate Journal

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Regulatory Influences on the Glycosylation of Rhodopsin By Human and Bovine Retinas

Kean

Niu

1995

Degenerative Diseases of the Retina

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The yeast expression system for recombinant glycosyltransferases

Malissard¹,

Zeng²,

Berger³

1999

Glycotechnology

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Glycosyltransferases are increasingly being used for in vitro synthesis of oligosaccharides. Since these enzymes are difficult to purify from natural sources, expression systems for soluble forms of the recombinant enzymes have been developed. This review focuses on the current state of development of yeast expression systems. Two yeast species have mainly been used, i.e. Saccharomyces cerevisiae and Pichia pastoris. Safety and ease of fermentation are well recognized for S. cerevisiae as a biotechnological expression system; however, even soluble forms of recombinant glycosyltransferases are not secreted. In some cases, hyperglycosylation may occur. P. pastoris, by contrast, secrete soluble orthoglycosylated forms to the supernatant where they can be recovered in a highly purified form.The review also covers some basic features of yeast fermentation and describes in some detail those glycosyltransferases that have successfully been expressed in yeasts. These include b1,4galactosyltransferase, a2,6sialyltransferase, a2,3sialyltransferase, a1,3fucosyltransferase III and VI and a1,2mannosyltransferase. Current efforts in introducing glycosylation systems of higher eukaryotes into yeasts are briefly addressed.

show abstract

In vitro galactosylation of rhodopsin and opsin: Kinetics, properties and characterization

Cited by 8 publications

References 49 publications

Untitled

Untitled

Regulatory Influences on the Glycosylation of Rhodopsin By Human and Bovine Retinas

The yeast expression system for recombinant glycosyltransferases

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