| dc.contributor.author |
Tsamadis, G |
en |
| dc.contributor.author |
Papageorgakopoulou, N |
en |
| dc.contributor.author |
Clonis, Y |
en |
| dc.date.accessioned |
2014-06-06T06:42:14Z |
|
| dc.date.available |
2014-06-06T06:42:14Z |
|
| dc.date.issued |
1992 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1007/BF00369548 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/501 |
|
| dc.subject |
Enzyme |
en |
| dc.subject |
Lactate Dehydrogenase |
en |
| dc.subject |
Pyruvate Kinase |
en |
| dc.subject |
Scaling Up |
en |
| dc.subject |
Ionic Strength |
en |
| dc.subject |
Specific Activity |
en |
| dc.title |
Downstream processing of diagnostic enzymes: Optimised protocols for the simultaneous separation and purification of lactate dehydrogenase and pyruvate kinase from rabbit muscle |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1007/BF00369548 |
en |
| heal.publicationDate |
1992 |
en |
| heal.abstract |
Cibacron Blue 3GA-Sepharose CL6B was used to design two optimised, inexpensive and easy to scale-up processes for the simultaneous separation and purification of l-lactate dehydrogenase (LDH) and pyruvate kinase (PK) from rabbit muscles. The tissue was homogenised, filtered, and the liquid treated by DEAE-cellulose and Sephadex-G25 gel to obtain the “pre-treated” extract which was used in the dye-column. The first |
en |
| heal.journalName |
Bioprocess and Biosystems Engineering |
en |
| dc.identifier.doi |
10.1007/BF00369548 |
en |