1,720,995 research outputs found

    Studio della frazione volatile del vino "primitivo" e tecnologie di produzione

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    Si espongono i risultati relativi ad un lavoro di comparazione di due tecniche di vinificazione e vengono comparati i dati ottenuti dall'estrazione SBSE-TDS-CIS della frazione volatile

    ELECTROPHORETIC AND CHROMATOGRAPHIC EVIDENCE FOR ALLELIC POLYMORPHISMS IN THE RIVER BUFFALO ALPHA-GLOBIN GENE-COMPLEX

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    Isoelectric focusing in the ultranarrow immobilized (7.1-7.5) pH gradient (IPG) of hemoglobin and high-performances liquid chromatography (HPLC) of globin chains were used to investigate Hb polymorphism in Italian river buffalo. Six different phenotypes, each characterized by two or four different Hbs, were detected by IPG, whereas two different II-alpha-globin chains were separated from two different I-alpha-chains by HPLC. Two alpha-chains (I-alpha-1 and II-alpha-3), and Hbs with similar mobilities (Hb1 and Hb3), were associated with the AA Hb phenotype: two alpha-chains (I-alpha-2 and II-alpha-4), and Hbs with different mobilities (Hb2 and Hb4), were associated with the BB phenotype: two sets of doublet Hbs were associated with the AB phenotype, thus suggesting allelic polymorphisms at the two alpha loci. An allele at the beta locus is responsible for increasing to as many as eight the number of different Hbs, thus further complicating the notable Hb polymorphism of the river buffalo

    Primary structure of alpha-globin chains from river buffalo (Bubalus bubalis L.) hemoglobins

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    Primary structure analysis of the four river buffalo alpha -globin chains showed that haplotypes A and B differ from each other by a substitution at codon 64 that may encode Ala or Asn. The A haplotype encodes two a-globin chains, (I)alpha1 and (II)alpha3, which differ at positions 129 and 131: (I)alpha1 has 64 Ala, 129 Phe, 131 Asn; (II)alpha3 has 64 Ala, 129 Leu, 131 Ser. The B haplotype encodes two alpha -globin chains, (I)alpha2 and (II)alpha4, which differ at positions 10 and 11: (I)alpha2 has 10 Ile, 11 Gln, 64 Asn; (II)alpha4 has 10 Val, 11 Lys, 64 Asn. Apart from the Ala/Asn polymorphism at position 64, amino acid substitutions in allelic and nonallelic alpha -globin chains seem to have arisen by single point mutations. Detection of electrophoretically silent mutations due to neutral amino acid substitutions and their influence on the isoelectric point are discussed. Furthermore, primary structures of river buffalo alpha -globin chains are compared to other species of the Bovidae family to suggest evolutionary events that have characterized the amino acid substitutions of river buffalo hemoglobin
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