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Interaction of hexokinase with the outer mitochondrial membrane and a hydrophobic matrix
The major portion of rat brain hexokinase (HK type 1) is bound to the outer membrane of mitochondria and glucose-6-phosphate (G6P) can release the bound enzyme. In an attempt to look at the 'hydrophobic' component of binding, interaction of the enzyme with a purely hydrophobic matrix, palm...
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| Published in: | Molecular and cellular biochemistry 2001-07, Vol.223 (1-2), p.81-87 |
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| container_end_page | 87 |
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| container_title | Molecular and cellular biochemistry |
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| creator | Ehsani-Zonouz, A Golestani, A Nemat-Gorgani, M |
| description | The major portion of rat brain hexokinase (HK type 1) is bound to the outer membrane of mitochondria and glucose-6-phosphate (G6P) can release the bound enzyme. In an attempt to look at the 'hydrophobic' component of binding, interaction of the enzyme with a purely hydrophobic matrix, palmityl-substituted Sepharose-4B (Sepharose-lipid) was investigated. Hexokinase readily bound to this matrix with retention of its catalytic activity. Glucose-6-phosphate which has a releasing effect on the mitochondrially bound enzyme, enhanced binding of the enzyme on the hydrophobic matrix. Chymotrypsin treatment of hexokinase which causes loss of binding to mitochondria, also results in loss of adsorption to the hydrophobic matrix, thus demonstrating that the 'hydrophobic tail' present at its N-terminal end is essential for binding in both cases. Data presented provide some new information relevant to understanding how hexokinase interacts with its natural binding matrix, the mitochondrion. |
| doi_str_mv | 10.1023/A:1017952827675 |
| format | article |
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In an attempt to look at the 'hydrophobic' component of binding, interaction of the enzyme with a purely hydrophobic matrix, palmityl-substituted Sepharose-4B (Sepharose-lipid) was investigated. Hexokinase readily bound to this matrix with retention of its catalytic activity. Glucose-6-phosphate which has a releasing effect on the mitochondrially bound enzyme, enhanced binding of the enzyme on the hydrophobic matrix. Chymotrypsin treatment of hexokinase which causes loss of binding to mitochondria, also results in loss of adsorption to the hydrophobic matrix, thus demonstrating that the 'hydrophobic tail' present at its N-terminal end is essential for binding in both cases. Data presented provide some new information relevant to understanding how hexokinase interacts with its natural binding matrix, the mitochondrion.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1023/A:1017952827675</identifier><identifier>PMID: 11681725</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Adsorption ; Animals ; Brain - cytology ; Brain - enzymology ; Catalysis ; Chromatography, Agarose - methods ; Chymotrypsin - metabolism ; Glucose-6-Phosphate - metabolism ; Hexokinase - metabolism ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes - enzymology ; Magnesium - metabolism ; Male ; Mitochondria - enzymology ; Polyamines - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Rats ; Rats, Inbred Strains ; Sepharose - analogs & derivatives ; Sepharose - metabolism ; Spermine - metabolism</subject><ispartof>Molecular and cellular biochemistry, 2001-07, Vol.223 (1-2), p.81-87</ispartof><rights>Kluwer Academic Publishers 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c280t-5d26614a26f53f42acd2617420ba44a52f7d3d61052a873846903c14a94491003</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11681725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ehsani-Zonouz, A</creatorcontrib><creatorcontrib>Golestani, A</creatorcontrib><creatorcontrib>Nemat-Gorgani, M</creatorcontrib><title>Interaction of hexokinase with the outer mitochondrial membrane and a hydrophobic matrix</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><description>The major portion of rat brain hexokinase (HK type 1) is bound to the outer membrane of mitochondria and glucose-6-phosphate (G6P) can release the bound enzyme. In an attempt to look at the 'hydrophobic' component of binding, interaction of the enzyme with a purely hydrophobic matrix, palmityl-substituted Sepharose-4B (Sepharose-lipid) was investigated. Hexokinase readily bound to this matrix with retention of its catalytic activity. Glucose-6-phosphate which has a releasing effect on the mitochondrially bound enzyme, enhanced binding of the enzyme on the hydrophobic matrix. Chymotrypsin treatment of hexokinase which causes loss of binding to mitochondria, also results in loss of adsorption to the hydrophobic matrix, thus demonstrating that the 'hydrophobic tail' present at its N-terminal end is essential for binding in both cases. Data presented provide some new information relevant to understanding how hexokinase interacts with its natural binding matrix, the mitochondrion.</description><subject>Adsorption</subject><subject>Animals</subject><subject>Brain - cytology</subject><subject>Brain - enzymology</subject><subject>Catalysis</subject><subject>Chromatography, Agarose - methods</subject><subject>Chymotrypsin - metabolism</subject><subject>Glucose-6-Phosphate - metabolism</subject><subject>Hexokinase - metabolism</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Intracellular Membranes - enzymology</subject><subject>Magnesium - metabolism</subject><subject>Male</subject><subject>Mitochondria - enzymology</subject><subject>Polyamines - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Sepharose - analogs & derivatives</subject><subject>Sepharose - 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| ispartof | Molecular and cellular biochemistry, 2001-07, Vol.223 (1-2), p.81-87 |
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| language | eng |
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| subjects | Adsorption Animals Brain - cytology Brain - enzymology Catalysis Chromatography, Agarose - methods Chymotrypsin - metabolism Glucose-6-Phosphate - metabolism Hexokinase - metabolism Hydrophobic and Hydrophilic Interactions Intracellular Membranes - enzymology Magnesium - metabolism Male Mitochondria - enzymology Polyamines - metabolism Protein Binding Protein Structure, Tertiary Proteins Rats Rats, Inbred Strains Sepharose - analogs & derivatives Sepharose - metabolism Spermine - metabolism |
| title | Interaction of hexokinase with the outer mitochondrial membrane and a hydrophobic matrix |
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