Linked Life Data

38219

Source:http://linkedlifedata.com/resource/pubmed/id/38219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1979-10-17
pubmed:abstractText
The radical anions (SCN)2.- and Br2.- produced during a pulse radiolysis of the respective potassium salts have been used to study the tryptophan residues of the glucoenzyme, glucoamylase I (EC 3.2.1.3.). At neutral pH, Br2.- reacted with the tryptophan residues of glucoamylase I as expected from previous studies of proteins and free amino acids. However, (SCN)2.- at neutral and high pH was surprisingly unreactive towards the native enzyme. Reaction did occur, however, between (SCN)2.- and glucoamylase from which one-third of the covalently bound carbohydrate had been removed, producing a tryptophyl radical. Reaction also occured between (SCN)2.- and glucoamylase I inactivated by treatment with sodium dodecyl sulphate, but the tryptophan residues were not involved. It is concluded from the results that two 'types' of tryptophan residues are found in glucoamylase I; both are attacked by Br2.- but only one type is attacked by (SCN)2.-.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0020-7616
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-8
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Interaction of radical anion probes with glucoamylase I from Aspergillus niger.
pubmed:publicationType
Journal Article