J H Calvo, N L Lopez-Corrales, R Osta, T M Skinner, S I Anderson, C Rodellar, P Zaragoza, A L Archibald
{"title":"猪2号染色体(2q21)上麦芽糖淀粉酶(MGAM)的荧光原位杂交和遗传作图鉴定。","authors":"J H Calvo, N L Lopez-Corrales, R Osta, T M Skinner, S I Anderson, C Rodellar, P Zaragoza, A L Archibald","doi":"10.1159/000056777","DOIUrl":null,"url":null,"abstract":"Maltase glucoamylase, one of the major constituents of the intestinal microvillar membrane (Norén et al., 1986), together with sucrase-isomaltase, has a role in the final digestion of starch. It has been hypothesized that human maltase glucoamylase activity serves as an alternative pathway for starch digestion when lumenal alpha-amylase activity is reduced as a result of immaturity or malnutrition and that maltase glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides (Nichols et al., 1998). The human MGAM gene has been cloned, sequenced and located to chromosome 7 (HSA7) (Nichols et al., 1998), but as yet, the porcine MGAM gene has not been mapped. We report the localization of the porcine MGAM gene to porcine (SSC) chromosome 2 by fluorescent in situ hybridization and linkage analysis. This assignment represents the first evidence of homology between SCC2 and HSA7.","PeriodicalId":10982,"journal":{"name":"Cytogenetics and cell genetics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000056777","citationCount":"3","resultStr":"{\"title\":\"Assignment of maltase glucoamylase (MGAM) to pig chromosome 2 (2q21) by fluorescence in situ hybridization and confirmation by genetic mapping.\",\"authors\":\"J H Calvo, N L Lopez-Corrales, R Osta, T M Skinner, S I Anderson, C Rodellar, P Zaragoza, A L Archibald\",\"doi\":\"10.1159/000056777\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Maltase glucoamylase, one of the major constituents of the intestinal microvillar membrane (Norén et al., 1986), together with sucrase-isomaltase, has a role in the final digestion of starch. It has been hypothesized that human maltase glucoamylase activity serves as an alternative pathway for starch digestion when lumenal alpha-amylase activity is reduced as a result of immaturity or malnutrition and that maltase glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides (Nichols et al., 1998). The human MGAM gene has been cloned, sequenced and located to chromosome 7 (HSA7) (Nichols et al., 1998), but as yet, the porcine MGAM gene has not been mapped. We report the localization of the porcine MGAM gene to porcine (SSC) chromosome 2 by fluorescent in situ hybridization and linkage analysis. This assignment represents the first evidence of homology between SCC2 and HSA7.\",\"PeriodicalId\":10982,\"journal\":{\"name\":\"Cytogenetics and cell genetics\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000056777\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cytogenetics and cell genetics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000056777\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cytogenetics and cell genetics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000056777","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Assignment of maltase glucoamylase (MGAM) to pig chromosome 2 (2q21) by fluorescence in situ hybridization and confirmation by genetic mapping.
Maltase glucoamylase, one of the major constituents of the intestinal microvillar membrane (Norén et al., 1986), together with sucrase-isomaltase, has a role in the final digestion of starch. It has been hypothesized that human maltase glucoamylase activity serves as an alternative pathway for starch digestion when lumenal alpha-amylase activity is reduced as a result of immaturity or malnutrition and that maltase glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides (Nichols et al., 1998). The human MGAM gene has been cloned, sequenced and located to chromosome 7 (HSA7) (Nichols et al., 1998), but as yet, the porcine MGAM gene has not been mapped. We report the localization of the porcine MGAM gene to porcine (SSC) chromosome 2 by fluorescent in situ hybridization and linkage analysis. This assignment represents the first evidence of homology between SCC2 and HSA7.