Literature DB >> 11945353

On the isolation, characterisation, and crystallisation of a human Bence-Jones protein of kappa type.

Walter H. Palm1.   

Abstract

The isolation and purification of the human Bence-Jones protein Rei is described. Physico-chemical data are given characterising the protein. It is shown that the protein could be crystallised. It is intended to use the crystals for single crystal X-ray diffraction studies.

Entities:  

Year:  1970        PMID: 11945353     DOI: 10.1016/0014-5793(70)80412-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  The structure determination of the variable portion of the Bence-Jones protein Au.

Authors:  H Fehlhammer; M Schiffer; O Epp; P M Colman; E E Lattman; P Schwager; W Steigemann; H J Schramm
Journal:  Biophys Struct Mech       Date:  1975-02-19

2.  Structural invariants of antigen binding: comparison of immunoglobulin VL-VH and VL-VL domain dimers.

Authors:  J Novotný; E Haber
Journal:  Proc Natl Acad Sci U S A       Date:  1985-07       Impact factor: 11.205

3.  Proteolytic excision and in situ cyclization of a bioactive loop from an REI-VL presentation scaffold.

Authors:  L R Helms; R Wetzel
Journal:  Protein Sci       Date:  1994-07       Impact factor: 6.725

Review 4.  Genetic determination of antibody specificity. Gene translocation and fusion, the molecular basis for the differentiation of the antibody-producing cell.

Authors:  N Hilschmann; H U Barnikol; H Kratzin; P Altevogt; M Engelhard; S Barnikol-Watanabe
Journal:  Naturwissenschaften       Date:  1978-12
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.