Bull semen nicotinamide adenine dinucleotide nucleosidase: VII. Nonenzymatic basis of apparent transglycosidation with histamine
The reaction between NAD and histamine in the presence of purified bull semen nicotinamide adenine dinucleotide nucleosidase (NADase) was studied with respect to the rate of disappearance of the nicotinamide ribosidic linkage of NAD and the rate of the loss of one orcinol-positive ribose of NAD. It...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1973-08, Vol.157 (2), p.446-450 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Anderson, Bruce M. Anderson, Constance D. Vercellotti, Sharon V. |
| description | The reaction between NAD and histamine in the presence of purified bull semen nicotinamide adenine dinucleotide nucleosidase (NADase) was studied with respect to the rate of disappearance of the nicotinamide ribosidic linkage of NAD and the rate of the loss of one orcinol-positive ribose of NAD. It was observed that in the presence of this enzyme, 50% of the ribosidic linkage was hydrolyzed prior to any change in orcinol-positive ribose. A nonenzymatic reaction of the product of hydrolysis, adenosine diphosphoribose with histamine was observed to result in the loss of one orcinol-positive ribose. Similar nonenzymatic reactions of histamine were observed with ribose and ribose-5-phosphate. The data suggest that the bull semen NADase does not catalyze a transglycosidation reaction between NAD and histamine as had been claimed previously. |
| doi_str_mv | 10.1016/0003-9861(73)90660-7 |
| format | Article |
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Nonenzymatic basis of apparent transglycosidation with histamine</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Anderson, Bruce M. ; Anderson, Constance D. ; Vercellotti, Sharon V.</creator><creatorcontrib>Anderson, Bruce M. ; Anderson, Constance D. ; Vercellotti, Sharon V.</creatorcontrib><description>The reaction between NAD and histamine in the presence of purified bull semen nicotinamide adenine dinucleotide nucleosidase (NADase) was studied with respect to the rate of disappearance of the nicotinamide ribosidic linkage of NAD and the rate of the loss of one orcinol-positive ribose of NAD. It was observed that in the presence of this enzyme, 50% of the ribosidic linkage was hydrolyzed prior to any change in orcinol-positive ribose. A nonenzymatic reaction of the product of hydrolysis, adenosine diphosphoribose with histamine was observed to result in the loss of one orcinol-positive ribose. Similar nonenzymatic reactions of histamine were observed with ribose and ribose-5-phosphate. The data suggest that the bull semen NADase does not catalyze a transglycosidation reaction between NAD and histamine as had been claimed previously.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(73)90660-7</identifier><identifier>PMID: 4354320</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Diphosphate ; Animals ; Cattle ; Cyanides ; Histamine ; Hydrogen-Ion Concentration ; Indicators and Reagents ; Kinetics ; Male ; N-Glycosyl Hydrolases - metabolism ; NAD ; Nucleoside Diphosphate Sugars ; Ribose ; Semen - enzymology ; Spectrophotometry ; Time Factors</subject><ispartof>Archives of biochemistry and biophysics, 1973-08, Vol.157 (2), p.446-450</ispartof><rights>1973</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986173906607$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4354320$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anderson, Bruce M.</creatorcontrib><creatorcontrib>Anderson, Constance D.</creatorcontrib><creatorcontrib>Vercellotti, Sharon V.</creatorcontrib><title>Bull semen nicotinamide adenine dinucleotide nucleosidase: VII. Nonenzymatic basis of apparent transglycosidation with histamine</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The reaction between NAD and histamine in the presence of purified bull semen nicotinamide adenine dinucleotide nucleosidase (NADase) was studied with respect to the rate of disappearance of the nicotinamide ribosidic linkage of NAD and the rate of the loss of one orcinol-positive ribose of NAD. It was observed that in the presence of this enzyme, 50% of the ribosidic linkage was hydrolyzed prior to any change in orcinol-positive ribose. A nonenzymatic reaction of the product of hydrolysis, adenosine diphosphoribose with histamine was observed to result in the loss of one orcinol-positive ribose. Similar nonenzymatic reactions of histamine were observed with ribose and ribose-5-phosphate. The data suggest that the bull semen NADase does not catalyze a transglycosidation reaction between NAD and histamine as had been claimed previously.</description><subject>Adenosine Diphosphate</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cyanides</subject><subject>Histamine</subject><subject>Hydrogen-Ion Concentration</subject><subject>Indicators and Reagents</subject><subject>Kinetics</subject><subject>Male</subject><subject>N-Glycosyl Hydrolases - metabolism</subject><subject>NAD</subject><subject>Nucleoside Diphosphate Sugars</subject><subject>Ribose</subject><subject>Semen - enzymology</subject><subject>Spectrophotometry</subject><subject>Time Factors</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9UU1P3DAQtVCrZaH8Ayr5VMEh4ImzjtNDpbKiZSUEl9Kr5dgTGJQ429gpWk789Ga7K07zNO_Nh95j7BTEBQhQl0IImVVawVkpzyuhlMjKAzYHUalMSF18YPN3ySE7ivFZCIBC5TM2K-SikLmYs7ersW15xA4DD-T6RMF25JFbj4ECck9hdC1OxNTcwUjeRvzKf69WF_yuDxheN51N5HhtI0XeN9yu13bAkHgabIiP7cb9n0rUB_5C6Yk_UUzToYCf2MfGthFP9vWYPfy4_rW8yW7vf66W328zhFKlzFu98FKBLJsKPWBZVLlucgfKNdaDqkHbWhe1BlX52iqPeb4ADdpJi4UAecy-7Pauh_7PiDGZjqLDtrUB-zEanQsQhaom4ee9cKw79GY9UGeHjdlbNvHfdjxO3_4lHEx0hMGhpwFdMr4nA8JsIzJb_83Wf1NOdRvRBP4BILyFOA</recordid><startdate>197308</startdate><enddate>197308</enddate><creator>Anderson, Bruce M.</creator><creator>Anderson, Constance D.</creator><creator>Vercellotti, Sharon V.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>197308</creationdate><title>Bull semen nicotinamide adenine dinucleotide nucleosidase: VII. Nonenzymatic basis of apparent transglycosidation with histamine</title><author>Anderson, Bruce M. ; Anderson, Constance D. ; Vercellotti, Sharon V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e176t-da85d36137f9ed1e74928f2c16cfad16b18ab84b8169dba6de2251818c3ae4013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Adenosine Diphosphate</topic><topic>Animals</topic><topic>Cattle</topic><topic>Cyanides</topic><topic>Histamine</topic><topic>Hydrogen-Ion Concentration</topic><topic>Indicators and Reagents</topic><topic>Kinetics</topic><topic>Male</topic><topic>N-Glycosyl Hydrolases - metabolism</topic><topic>NAD</topic><topic>Nucleoside Diphosphate Sugars</topic><topic>Ribose</topic><topic>Semen - enzymology</topic><topic>Spectrophotometry</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anderson, Bruce M.</creatorcontrib><creatorcontrib>Anderson, Constance D.</creatorcontrib><creatorcontrib>Vercellotti, Sharon V.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anderson, Bruce M.</au><au>Anderson, Constance D.</au><au>Vercellotti, Sharon V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bull semen nicotinamide adenine dinucleotide nucleosidase: VII. Nonenzymatic basis of apparent transglycosidation with histamine</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1973-08</date><risdate>1973</risdate><volume>157</volume><issue>2</issue><spage>446</spage><epage>450</epage><pages>446-450</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The reaction between NAD and histamine in the presence of purified bull semen nicotinamide adenine dinucleotide nucleosidase (NADase) was studied with respect to the rate of disappearance of the nicotinamide ribosidic linkage of NAD and the rate of the loss of one orcinol-positive ribose of NAD. It was observed that in the presence of this enzyme, 50% of the ribosidic linkage was hydrolyzed prior to any change in orcinol-positive ribose. A nonenzymatic reaction of the product of hydrolysis, adenosine diphosphoribose with histamine was observed to result in the loss of one orcinol-positive ribose. Similar nonenzymatic reactions of histamine were observed with ribose and ribose-5-phosphate. The data suggest that the bull semen NADase does not catalyze a transglycosidation reaction between NAD and histamine as had been claimed previously.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4354320</pmid><doi>10.1016/0003-9861(73)90660-7</doi><tpages>5</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1973-08, Vol.157 (2), p.446-450 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Diphosphate Animals Cattle Cyanides Histamine Hydrogen-Ion Concentration Indicators and Reagents Kinetics Male N-Glycosyl Hydrolases - metabolism NAD Nucleoside Diphosphate Sugars Ribose Semen - enzymology Spectrophotometry Time Factors |
| title | Bull semen nicotinamide adenine dinucleotide nucleosidase: VII. Nonenzymatic basis of apparent transglycosidation with histamine |
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