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Canova-Davis E, Baldonado IP, Moore JA, et al. Properties of a cleaved two-chain form of recombinant human growth hormone. Int J Pept Protein Res. 1990;35(1):17-24doi: 10.1111/j.1399-3011.1990.tb00716.x.
Canova-Davis, E., Baldonado, I. P., Moore, J. A., Rudman, C. G., Bennett, W. F., & Hancock, W. S. (1990). Properties of a cleaved two-chain form of recombinant human growth hormone. International journal of peptide and protein research, 35(1), 17-24. https://doi.org/10.1111/j.1399-3011.1990.tb00716.x
Canova-Davis, E, et al. "Properties of a cleaved two-chain form of recombinant human growth hormone." International journal of peptide and protein research vol. 35,1 (1990): 17-24. doi: https://doi.org/10.1111/j.1399-3011.1990.tb00716.x
Canova-Davis E, Baldonado IP, Moore JA, Rudman CG, Bennett WF, Hancock WS. Properties of a cleaved two-chain form of recombinant human growth hormone. Int J Pept Protein Res. 1990 Jan;35(1):17-24. doi: 10.1111/j.1399-3011.1990.tb00716.x. PMID: 2182557.
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Int J Pept Protein Res. 1990 Jan;35(1):17-24. doi: 10.1111/j.1399-3011.1990.tb00716.x.

Properties of a cleaved two-chain form of recombinant human growth hormone.

International journal of peptide and protein research

E Canova-Davis, I P Baldonado, J A Moore, C G Rudman, W F Bennett, W S Hancock

Affiliations

  1. Genentech, Inc., South San Francisco, California.

PMID: 2182557 DOI: 10.1111/j.1399-3011.1990.tb00716.x

Abstract

Escherichia coli cells transformed with plasmids engineered for the expression of recombinant human growth hormone as a secreted product also produced a proteolytically cleaved form of rhGH. This variant is isolated at a high resolution anion exchange chromatography stage during the manufacturing process. The higher isoelectric point of this form is demonstrated by isoelectric focusing and chromatofocusing and the two-chain nature by tryptic mapping, N- and C-terminal sequence analyses, and sodium dodecyl sulfate polyacrylamide gel electrophoresis. These data indicate that the single site of cleavage is between Thr-142 and Tyr-143, in contrast to the two-chain variant isolated from human pituitary glands, which has a clip after residue Phe-139. The recombinant two-chain form was further characterized by reversed-phase high performance liquid chromatography at both acidic and basic pHs. The assay utilizing bicarbonate-containing mobile phases was determined to be the most efficient and sensitive method. The bioactivity of this two-chain form was measured by the in vivo rat weight gain assay and by the in vitro Nb2 cell bioassay. Its immunological similarity to intact one-chain rhGH was demonstrated with an enzyme-linked immunosorbent assay.

Cited by

Crowell LE, Lu AE, Love KR, Stockdale A, Timmick SM, Wu D, Wang YA, Doherty W, Bonnyman A, Vecchiarello N, Goodwine C, Bradbury L, Brady JR, Clark JJ, Colant NA, Cvetkovic A, Dalvie NC, Liu D, Liu Y, Mascarenhas CA, Matthews CB, Mozdzierz NJ, Shah KA, Wu SL, Hancock WS, Braatz RD, Cramer SM, Love JC.
Nat Biotechnol. 2018 Oct 01; doi: 10.1038/nbt.4262. Epub 2018 Oct 01.
PMID: 30272677

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