## Abstract Endoglucanase (C~__x__~ cellulase) and cellobiase are often crossβcontaminated in separation procedures by ionβexchange chromatography such as DEAEβcellulose. By using concanavalin A (Con A)βagarose chromatography, C~__x__~ cellulase and cellobiase from __Trichoderma viride__ can be sep
Chromatography of renin substrate on concanavalin A-agarose
β Scribed by Morton P. Printz; Timothy J. Gregory; John A. Lewicki; Jana M. Printz
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 479 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
Renin substrate, the serum prohormone of angiotensin, is a glycoprotein which is shown to bind to concanavalin A. This interaction permits the use of lectin affinity chromatography in overcoming a major problem in the protein's purification, namely the separation of renin substrate from albumin and similar serum proteins. Low concentrations of either a-methyl mannoside or o-glucose displace renin substrate from the affinity column with no significant loss of pharmacological activity.
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This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A .,03:A280 ratios ranging from 0.62 to 2.45 were purified to AIOa:AZSO ratios ranging from approximately 2.8 to 3.1 with
## Abstract Baculovirus has emerged as a novel gene delivery and vaccine vector, and the demand for purified baculovirus is rising due to the increasing in vivo applications. Since the baculoviral envelope protein gp64 is a glycoprotein, we aimed to develop a concanavalin A (Con A) chromatography p