Purification of soluble invertase from potato
Burch, L.R. ; Davies, H.V. ; Cuthbert, E.M. ; Machray, E.C. ; Hedley, P. ; Waugh, R.
Amsterdam : Elsevier
Amsterdam : Elsevier
| ISSN: |
0031-9422
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|---|---|
| Keywords: |
Solanaceae ; Solanum tuberosum ; invertase ; potato ; purification.
|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798291225506217984 |
|---|---|
| autor | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| autorsonst | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0031-9422(92)80331-8 |
| datenlieferant | nat_lic_papers |
| fussnote | Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 M"r polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The K"m (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (K"m 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (K"m 9.2 mM), raffinose (K"m 7.1 mM) and trehalose (K"m 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase. |
| hauptsatz | hsatz_simple |
| identnr | NLZ175776539 |
| issn | 0031-9422 |
| journal_name | Phytochemistry |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 31 (1992), S. 1901-1904 |
| schlagwort | Solanaceae Solanum tuberosum invertase potato purification. |
| search_space | articles |
| shingle_author_1 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| shingle_author_2 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| shingle_author_3 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| shingle_author_4 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. |
| shingle_catch_all_1 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. Purification of soluble invertase from potato Solanaceae Solanum tuberosum invertase potato purification. Solanaceae Solanum tuberosum invertase potato purification. 0031-9422 00319422 Elsevier |
| shingle_catch_all_2 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. Purification of soluble invertase from potato Solanaceae Solanum tuberosum invertase potato purification. Solanaceae Solanum tuberosum invertase potato purification. 0031-9422 00319422 Elsevier |
| shingle_catch_all_3 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. Purification of soluble invertase from potato Solanaceae Solanum tuberosum invertase potato purification. Solanaceae Solanum tuberosum invertase potato purification. 0031-9422 00319422 Elsevier |
| shingle_catch_all_4 | Burch, L.R. Davies, H.V. Cuthbert, E.M. Machray, E.C. Hedley, P. Waugh, R. Purification of soluble invertase from potato Solanaceae Solanum tuberosum invertase potato purification. Solanaceae Solanum tuberosum invertase potato purification. 0031-9422 00319422 Elsevier |
| shingle_title_1 | Purification of soluble invertase from potato |
| shingle_title_2 | Purification of soluble invertase from potato |
| shingle_title_3 | Purification of soluble invertase from potato |
| shingle_title_4 | Purification of soluble invertase from potato |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:29:14.242Z |
| titel | Purification of soluble invertase from potato |
| titel_suche | Purification of soluble invertase from potato Proteins with acid invertase activity have been identified from potato (Solanum tuberosum L.) leaves and tubers, and purified to near homogeneity. Under denaturing conditions (SDS-PAGE) the purified invertase is associated in each case with a 58 000 M"r polypeptide. A pI of pH 5.2 was determined for the tuber enzyme and both invertases had a pH optimum of 5. The K"m (sucrose) was 7.9 mM for the tuber enzyme and 2.4 mM for the leaf enzyme. In addition, leaf invertase also hydrolysed lactose (K"m 6.4 mM) at approximately 10% of the rate of sucrose. Tuber invertase also hydrolysed lactose (K"m 9.2 mM), raffinose (K"m 7.1 mM) and trehalose (K"m 0.66 mM), again at a rate approximately 10% that of sucrose. Product inhibition by fructose was linear mixed for the leaf enzyme and competitive for the tuber enzyme. Glucose inhibition was uncompetitive for the leaf enzyme and non-competitive for tuber invertase. |
| topic | W V |
| uid | nat_lic_papers_NLZ175776539 |