<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ArticleSet PUBLIC "-//NLM//DTD PubMed 2.7//EN" "https://dtd.nlm.nih.gov/ncbi/pubmed/in/PubMed.dtd">
<ArticleSet>
<Article>
<Journal>
				<PublisherName>University of Tehran</PublisherName>
				<JournalTitle>Journal of Sciences, Islamic Republic of Iran</JournalTitle>
				<Issn>1016-1104</Issn>
				<Volume>3</Volume>
				<Issue>2</Issue>
				<PubDate PubStatus="epublish">
					<Year>1992</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>THE CALCIUM BINDING SITES OF THE
BAKERS&#039; YEAST TRANSKETOLASE</ArticleTitle>
<VernacularTitle>-</VernacularTitle>
			<FirstPage></FirstPage>
			<LastPage></LastPage>
			<ELocationID EIdType="pii">31510</ELocationID>
			
			
			<Language>EN</Language>
<AuthorList>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
		    <Abstract>The calcium binding sites of Bakers&#039; Yeast Transketolase (TK) was elucidated
by estimating the pKa values of the functional groups that bind to calcium. These
pKa&#039;s were found to be 6.25 and 7.2 relating to the pKa&#039;s of the two immidazol
moieties of histidine residues on the enzyme. The rate of the binding of calcium to
the enzyme was obtained separately as a function of pH. Maximum values were
obtained at the pKa&#039;s of the immidazol rings of histidine correlating closely with the
values obtained by direct titration. The activity rate studies as a function of pH
showed that the enzyme, when bound to its cofactors, becomes further activated
over and above the regular increasing trend of the pH rate profile at similar pH&#039;s
which are optimal for calcium binding</Abstract>
<ArchiveCopySource DocType="pdf">https://jsciences.ut.ac.ir/article_31510_5b9a8d01164ae511a4d6f8c83b041556.pdf</ArchiveCopySource>
</Article>
</ArticleSet>
