Manufacture and use of polypeptides tagged using binding molecul

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

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5303873, 530402, 435 71, 435 691, C07K 100, C12P 2108, C12P 2106, G01N 3353

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active

061179760

ABSTRACT:
Molecules comprise (i) a polypeptide (such as calmodulin) which has calcium-dependent binding affinity for ligand and (ii) another polypeptide, the polypeptides preferably being joined by a peptide bond and produced by recombinant expression from a gene fusion. The molecules are useful in detection, immobilization, targeting and purification, cell-labelling, and band-shift assays for determining binding of a member of a specific binding pair (sbp) for complementary sbp member. For purposes of band-shift assays, polypeptide (i) need not have calcium-dependent binding affinity for a ligand, but should have a dissociation constant for a ligand of 10 nM or less, measured at a pH of between 6 and 9 at 20.degree. C. In an alternative embodiment, a calmodulin-binding polypeptide which is, or is derived from, mastoparan is joined, as polypeptide (i) instead of a binding polypeptide, to the other polypeptide.

REFERENCES:
patent: 5498538 (1996-03-01), Kay et al.
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Beidler et al., "Cloning and High Level Expression of a Chemeric Antibody . . . ," Journal of Immunology, 141(11):4053-4060, Dec. 1988.
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Tomio Ono et al., "Molecular Cloning Sequence and Distribution of Rat Calspermin, a High Affinity Calmodulin-binding Protein," The Journal of Biological Chemistry, vol. 264, No. 4, pp. 2081-2087 (Feb. 5, 1989).
Rasera Da Silva et al., "Hybrid myosin light chains containing a calcium-specific site from toponin C," Chemical Abstracts, vol. 116, No. 12, p. 354 (Mar. 30, 1992), abstract no. 123563g.
MacKenzie, et al., "Biofunctional fusion proteins consisting of a single-chain antibody and an engineered lanthanide-binding protein," Immunotechnology, 1:139-150, 1995.
Neri et al., "Calmodulin as a Versatile Tag for Antibody Fragments," Biotechnology, 13:373-377, Apr. 1995.

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