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<ArticleSet>
<Article>
<Journal>
				<PublisherName>Iranian Biology Society</PublisherName>
				<JournalTitle>Journal of Plant Research 
(Iranian Journal of Biology)</JournalTitle>
				<Issn>2383-2592</Issn>
				<Volume>33</Volume>
				<Issue>1</Issue>
				<PubDate PubStatus="epublish">
					<Year>2020</Year>
					<Month>04</Month>
					<Day>20</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Identification of a protein that inhibit amylase activity in seed of wheat</ArticleTitle>
<VernacularTitle>Identification of a protein that inhibit amylase activity in seed of wheat</VernacularTitle>
			<FirstPage>70</FirstPage>
			<LastPage>82</LastPage>
			<ELocationID EIdType="pii">1430</ELocationID>
			
			
			<Language>FA</Language>
<AuthorList>
<Author>
					<FirstName>Masoud</FirstName>
					<LastName>Haidarizadeh</LastName>
<Affiliation>Faculty member of departement of Biology,University of Kurdistan</Affiliation>

</Author>
<Author>
					<FirstName>Fariba</FirstName>
					<LastName>Hasanvand</LastName>
<Affiliation>Department of Biological Science, University of Kurdistan, Sanandaj, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2018</Year>
					<Month>04</Month>
					<Day>24</Day>
				</PubDate>
			</History>
		<Abstract>Storage proteins which found in seeds of many plants are studied in various fields such as human and animal nutrition, chemistry of protein, pharmacology, plant biochemistry and medicinal plants. The ability of these compounds to cause nutritional problems and toxic effects when used as foods has led to several studies on their dispersion in plants. In this research, seed proteins of wheat (Zarrin variety) have been extracted. The protein of interest was purified by ammonium sulfate precipitation method; dialysis and ion exchange chromatography. After purification by Fast protein liquid chromatography (FPLC), electrophoretic properties of this protein were investigated by Sodium dodecyl-polyacrylamide gel electrophoresis )SDS-PAGE( method. Inhibitory activity of this Protein against Bacterial alpha-amylase and human saliva were measured using the Bernfeld method. FPLC diagram illustrates the purification and collection of the desired protein. The electrophoretic pattern of this protein with relative mobility of 0.60 and 0.59 confirmed the purification process. Hydrolytic activity of bacterial and human saliva Alpha- amylase decreased by this protein 89.97% and 97.07% respectively. In general the isolation, purification and alpha-amylase inhibition property of this protein which extracted from wheat seed were confirmed in this study. Inhibition of bacterial alpha-amylase by this protein can be considered by agricultural researchers in biological control of parasites and pests. This alpha-amylase inhibitor can also be used to treat diabetes, digestive deficiencies and modify dietary regimens to reduce weight.</Abstract>
			<OtherAbstract Language="FA">Storage proteins which found in seeds of many plants are studied in various fields such as human and animal nutrition, chemistry of protein, pharmacology, plant biochemistry and medicinal plants. The ability of these compounds to cause nutritional problems and toxic effects when used as foods has led to several studies on their dispersion in plants. In this research, seed proteins of wheat (Zarrin variety) have been extracted. The protein of interest was purified by ammonium sulfate precipitation method; dialysis and ion exchange chromatography. After purification by Fast protein liquid chromatography (FPLC), electrophoretic properties of this protein were investigated by Sodium dodecyl-polyacrylamide gel electrophoresis )SDS-PAGE( method. Inhibitory activity of this Protein against Bacterial alpha-amylase and human saliva were measured using the Bernfeld method. FPLC diagram illustrates the purification and collection of the desired protein. The electrophoretic pattern of this protein with relative mobility of 0.60 and 0.59 confirmed the purification process. Hydrolytic activity of bacterial and human saliva Alpha- amylase decreased by this protein 89.97% and 97.07% respectively. In general the isolation, purification and alpha-amylase inhibition property of this protein which extracted from wheat seed were confirmed in this study. Inhibition of bacterial alpha-amylase by this protein can be considered by agricultural researchers in biological control of parasites and pests. This alpha-amylase inhibitor can also be used to treat diabetes, digestive deficiencies and modify dietary regimens to reduce weight.</OtherAbstract>
		<ObjectList>
			<Object Type="keyword">
			<Param Name="value">" wheat"</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">" enzyme inhibitors"</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">" alpha-amylase"</Param>
			</Object>
		</ObjectList>
<ArchiveCopySource DocType="pdf">https://plant.ijbio.ir/article_1430_411ae1bf081d1674ca6091f8c59a266f.pdf</ArchiveCopySource>
</Article>
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