Regulation of cyclic nucleotide phosphodiesterase (PDE) by zein peptides
We have prepared zein peptides and characterized their ability to regulate the activity of cyclic nucleotide phosphodiesterase (PDE) isozymes obtained from canine heart ventricle. Native-zein inhibited 42%, 18% and 25% of the activities of PDE1, PDE2, and PDE4, respectively. AT1 was prepared by part...
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| Veröffentlicht in: | Nihon Shokuhin Kagaku Kōgaku kaishi 2000/03/15, Vol.47(3), pp.220-226 |
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| container_title | Nihon Shokuhin Kagaku Kōgaku kaishi |
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| creator | Kokean, Y. (Mie-ken. Government Office, Tsu (Japan)) Suzuki, K Funatsu, G Takahashi, T Mukai, J Naka, M Tanaka, T |
| description | We have prepared zein peptides and characterized their ability to regulate the activity of cyclic nucleotide phosphodiesterase (PDE) isozymes obtained from canine heart ventricle. Native-zein inhibited 42%, 18% and 25% of the activities of PDE1, PDE2, and PDE4, respectively. AT1 was prepared by partial hydrolysis of the native-zein with 0.3 N HCl at 50 degrees C for 24 hr. The AT1 increased the activities of 63% and 40% of PDE1 and PDE4. AT1 was hydrolyzed with pepsin, chymotrypsin, thermolysin, and subtilisin. Pepsin- and chymotrypsin-treated AT1 increased the activity of PDE1 by 75%. Deaminated-zein were prepared by mild HCl hydrolysis (with 0.2 N HCl at 55 degrees C for 5 hr). Deamidation of zein had no effect on the activities of PDE1, PDE3, and PDE4. However, a deaminated-zein fraction (DA-3) increased PDE2 activity by 16%. From these results, it was confirmed that zein peptides had regulatory effects on PDE isozymes |
| doi_str_mv | 10.3136/nskkk.47.220 |
| format | Article |
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(Mie-ken. Government Office, Tsu (Japan)) ; Suzuki, K ; Funatsu, G ; Takahashi, T ; Mukai, J ; Naka, M ; Tanaka, T</creator><creatorcontrib>Kokean, Y. (Mie-ken. Government Office, Tsu (Japan)) ; Suzuki, K ; Funatsu, G ; Takahashi, T ; Mukai, J ; Naka, M ; Tanaka, T</creatorcontrib><description>We have prepared zein peptides and characterized their ability to regulate the activity of cyclic nucleotide phosphodiesterase (PDE) isozymes obtained from canine heart ventricle. Native-zein inhibited 42%, 18% and 25% of the activities of PDE1, PDE2, and PDE4, respectively. AT1 was prepared by partial hydrolysis of the native-zein with 0.3 N HCl at 50 degrees C for 24 hr. The AT1 increased the activities of 63% and 40% of PDE1 and PDE4. AT1 was hydrolyzed with pepsin, chymotrypsin, thermolysin, and subtilisin. Pepsin- and chymotrypsin-treated AT1 increased the activity of PDE1 by 75%. Deaminated-zein were prepared by mild HCl hydrolysis (with 0.2 N HCl at 55 degrees C for 5 hr). Deamidation of zein had no effect on the activities of PDE1, PDE3, and PDE4. However, a deaminated-zein fraction (DA-3) increased PDE2 activity by 16%. From these results, it was confirmed that zein peptides had regulatory effects on PDE isozymes</description><identifier>ISSN: 1341-027X</identifier><identifier>EISSN: 1881-6681</identifier><identifier>DOI: 10.3136/nskkk.47.220</identifier><language>jpn</language><publisher>Japanese Society for Food Science and Technology</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ENZYMIC ACTIVITY ; FOSFODIESTERASA ; PEPTIDE ; PEPTIDES ; PEPTIDOS ; PHOSPHODIESTERASE ; PROLAMINAS ; PROLAMINE ; PROLAMINES</subject><ispartof>Nippon Shokuhin Kagaku Kogaku Kaishi, 2000/03/15, Vol.47(3), pp.220-226</ispartof><rights>Japanese Society for Food Science and Technology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Kokean, Y. 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Government Office, Tsu (Japan))</creatorcontrib><creatorcontrib>Suzuki, K</creatorcontrib><creatorcontrib>Funatsu, G</creatorcontrib><creatorcontrib>Takahashi, T</creatorcontrib><creatorcontrib>Mukai, J</creatorcontrib><creatorcontrib>Naka, M</creatorcontrib><creatorcontrib>Tanaka, T</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><jtitle>Nihon Shokuhin Kagaku Kōgaku kaishi</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kokean, Y. (Mie-ken. Government Office, Tsu (Japan))</au><au>Suzuki, K</au><au>Funatsu, G</au><au>Takahashi, T</au><au>Mukai, J</au><au>Naka, M</au><au>Tanaka, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of cyclic nucleotide phosphodiesterase (PDE) by zein peptides</atitle><jtitle>Nihon Shokuhin Kagaku Kōgaku kaishi</jtitle><addtitle>Nippon Shokuhin Kagaku Kogaku Kaishi</addtitle><date>2000-01-01</date><risdate>2000</risdate><volume>47</volume><issue>3</issue><spage>220</spage><epage>226</epage><pages>220-226</pages><issn>1341-027X</issn><eissn>1881-6681</eissn><abstract>We have prepared zein peptides and characterized their ability to regulate the activity of cyclic nucleotide phosphodiesterase (PDE) isozymes obtained from canine heart ventricle. Native-zein inhibited 42%, 18% and 25% of the activities of PDE1, PDE2, and PDE4, respectively. AT1 was prepared by partial hydrolysis of the native-zein with 0.3 N HCl at 50 degrees C for 24 hr. 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| ispartof | Nippon Shokuhin Kagaku Kogaku Kaishi, 2000/03/15, Vol.47(3), pp.220-226 |
| issn | 1341-027X 1881-6681 |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ENZYMIC ACTIVITY FOSFODIESTERASA PEPTIDE PEPTIDES PEPTIDOS PHOSPHODIESTERASE PROLAMINAS PROLAMINE PROLAMINES |
| title | Regulation of cyclic nucleotide phosphodiesterase (PDE) by zein peptides |
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