Determination of Disulfide Bonds in γ-46 Gliadin

نویسندگان

  • T. A. Egorov
  • T. I. Odintsova
  • A. K. Musolyamov
چکیده

—The disulfide bonds in γ-46 gliadin were identified: Cys 173 –Cys 192 , Cys 212 –Cys 291 , Cys 165 –Cys 199 (or Cys 200 ), Cys 283 –Cys 200 (or Cys 199 ). The disulfide-containing peptides were obtained by limited hydrolysis of the intact protein with chymotrypsin at an enzyme/substrate ratio of 1:1000 at 20°C for 22 h with subsequent digestion of disulfide-containing fragments with trypsin and chymotrypsin. The locations of disulfide bonds were determined by sequencing disulfide-containing fractions and constituent peptides and comparison of the obtained sequences with the partial amino acid sequence of γ-46 gliadin determined earlier.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Isolation and Characterization of Gliadin-Like Subunits from Glutenin

The polypeptide subunits of wheat glutenin obtained after reductive cleavage of disulfide bonds have been separated into two fractions by a modified Osborne technique. Approximately 62% of the subunits by weight are soluble, as is gliadin, in neutral 70% ethanol; the ethanol-soluble subunits are mainly of 44,000 molecular weight (MW). The ethanol-insoluble glutenin subunit fraction is markedly ...

متن کامل

Synthesis of Zinc Dimethyldithiocarbamate by Reductive Disulfide Bond Cleavage of Tetramethylthiuram Disulfide in Presence of Zn2+

The zinc(II) complex [Zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = N,N-dimethyldithiocarbamate; thiram = N,N-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. Surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with Zn2+ in methanolic media to give the [Z...

متن کامل

The natural occurrence of human fibrinogen variants disrupting inter-chain disulfide bonds (AaCys36Gly, AaCys36Arg and AaCys45Tyr) confirms the role of N-terminal Aa disulfide bonds in protein assembly and secretion

Fibrinogen is a 340-kDa dimeric protein, both halves being composed of three polypeptide chains (Aa, Bb, γ) encoded by a cluster of three genes. The combination leads to a molecule organized with a central E domain connected by stranded coiled-coils to two distal D domains. The coiled-coils are in the N-terminal portion of each Aa, Bb and γ chains. The chain assembly starts with either an Aa−γ ...

متن کامل

Isolation and phylogenetic analysis of novel γ-gliadin genes in genus Dasypyrum.

As the most ancient member of the wheat gluten family, the γ-gliadin genes are suitable for phylogenetic analysis among wheat and related species. Species in the grass genus Dasypyrum have been widely used for wheat cross breeding. However, the genomic relationships among Dasypyrum species have been little studied. We isolated 22 novel γ-gliadin gene sequences, among which 10 are putatively fun...

متن کامل

Recombinant Production of a Novel Fusion Protein: Listeriolysin O Fragment Fused to S1 Subunit Of Pertussis Toxin

Background: Some resources have suggested that genetically inactivated pertussis toxoid (PTs) bear a more protective effect than chemically inactivated products. This study aimed to produce new version of PT, by cloning an inactive pertussis toxin S1 subunit (PTS1) in a fusion form with N-terminal half of the listeriolysin O (LLO) pore-forming toxin. Methods: Deposited pdb structure file of the...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 1999