Literature DB >> 7702741

Purification and characterization of a high-molecular-weight form of recombinant human interleukin-2.

Z Ahmad1, D Ciolek, Y C Pan, H Michel, F R Khan.   

Abstract

During purification of recombinant Interleukin-2 (rIL-2) by reversed-phase HPLC, early fractions are discarded due to the presence of an unidentified form of rIL-2. A procedure has been developed to isolate and purify this unidentified form of rIL-2. The purification process involves two chromatography steps and utilizes a Bakerbond Carboxy-Sulfon (CS) column under two different conditions. This material, designated as a high-molecular-weight form of rIL-2 (HMWrIL-2), exhibits lower mobility during SDS-PAGE and has a pI which is approximately one unit less than that of rIL-2, but has similar bioactivity to rIL-2. Structural analysis through enzymatic cleavage, HPLC peptide mapping, mass spectrometry, sequencing, and amino acid composition revealed that the difference between these two proteins is a C-terminal extension of 11 amino acids. This extension could be the result of a nonstandard translation event.

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Year:  1994        PMID： 7702741     DOI： 10.1007/bf01890457

Source DB:  PubMed          Journal:  J Protein Chem        ISSN： 0277-8033


  14 in total

1.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

2.  Purification and characterization of recombinant human interleukin-2 produced in Escherichia coli.

Authors:  K Kato; T Yamada; K Kawahara; H Onda; T Asano; H Sugino; A Kakinuma
Journal:  Biochem Biophys Res Commun       Date:  1985-07-31       Impact factor: 3.575

3.  Interleukin-2 augments natural killer cell activity.

Authors:  C S Henney; K Kuribayashi; D E Kern; S Gillis
Journal:  Nature       Date:  1981-05-28       Impact factor: 49.962

4.  Effects of natural and recombinant IL 2 on regulation of IFN gamma production and natural killer activity: lack of involvement of the Tac antigen for these immunoregulatory effects.

Authors:  J R Ortaldo; A T Mason; J P Gerard; L E Henderson; W Farrar; R F Hopkins; R B Herberman; H Rabin
Journal:  J Immunol       Date:  1984-08       Impact factor: 5.422

5.  A gas-liquid solid phase peptide and protein sequenator.

Authors:  R M Hewick; M W Hunkapiller; L E Hood; W J Dreyer
Journal:  J Biol Chem       Date:  1981-08-10       Impact factor: 5.157

6.  Structure-function analysis of human interleukin-2. Identification of amino acid residues required for biological activity.

Authors:  G Ju; L Collins; K L Kaffka; W H Tsien; R Chizzonite; R Crowl; R Bhatt; P L Kilian
Journal:  J Biol Chem       Date:  1987-04-25       Impact factor: 5.157

7.  Structure-activity relationships of recombinant human interleukin 2.

Authors:  M P Weir; M A Chaplin; D M Wallace; C W Dykes; A N Hobden
Journal:  Biochemistry       Date:  1988-09-06       Impact factor: 3.162

8.  Use of N-chlorosuccinimide/urea for the selective cleavage of tryptophanyl peptide bonds in proteins. Cytochrome c.

Authors:  M A Lischwe; M T Sung
Journal:  J Biol Chem       Date:  1977-07-25       Impact factor: 5.157

9.  Sequencing of peptides and proteins from the carboxy terminus.

Authors:  V L Boyd; M Bozzini; G Zon; R L Noble; R J Mattaliano
Journal:  Anal Biochem       Date:  1992-11-01       Impact factor: 3.365

10.  Molecular cloning of human interleukin 2 cDNA and its expression in E. coli.

Authors:  R Devos; G Plaetinck; H Cheroutre; G Simons; W Degrave; J Tavernier; E Remaut; W Fiers
Journal:  Nucleic Acids Res       Date:  1983-07-11       Impact factor: 16.971
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