Literature DB >> 6749333

A radioimmunoassay for total human cathepsin B.

A D Recklies, J S Mort.   

Abstract

A radioimmunoassay for human cathepsin B is described, which demonstrates the usefulness of protein A-bearing Staphylococcus aureus as an immunosorbent in a system where the primary antibody IgG has a low binding affinity for protein A. The removal of bound antigen from the incubation mixture is achieved by the use of a rabbit second step antiserum which confers high binding affinity for protein A to the primary immune complex. This method, as employed in the assay for human cathepsin B, is very reproducible and economical for large numbers of samples. The use of a monospecific antiserum to human cathepsin B and slightly alkaline assay conditions allow the determination of total cathepsin B protein in tissue fluids which is not possible by enzyme activity determination.

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Year:  1982        PMID: 6749333     DOI: 10.1016/0009-8981(82)90121-8

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  2 in total

1.  Interrelationship of active and latent secreted human cathepsin B precursors.

Authors:  J S Mort; A D Recklies
Journal:  Biochem J       Date:  1986-01-01       Impact factor: 3.857

2.  A cysteine proteinase secreted from human breast tumours is immunologically related to cathepsin B.

Authors:  A D Recklies; A R Poole; J S Mort
Journal:  Biochem J       Date:  1982-12-01       Impact factor: 3.857

  2 in total

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