Hostname: page-component-77c89778f8-vsgnj Total loading time: 0 Render date: 2024-07-20T21:42:39.501Z Has data issue: false hasContentIssue false

Protection of T4 bacteriophage against inactivation during freezing and thawing by addition of peptides

Published online by Cambridge University Press:  19 October 2009

P. R. M. Steele
Affiliation:
University Department of Pathology, Cambridge, England
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Peptides of rabbit globin produced by tryptic digestion, were found to be highly protective against inactivation of freeze-thawed T4 phage. In concentrations of about 10−3 M the peptides protected the phage against inactivation by both concentrated NaBr in the unfrozen aqueous phase and the eutectic phase change.

Fractionation of the poptides by G25 Sephadex showed that peptide concentration rather than peptide size was the more important factor in determining the degree of protection of the phage by electrolyte effects. In contrast, protection against eutectic injury was strongly dependent on peptide size.

Possible mechanisms of action of the protective peptides are discussed.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1972

References

REFERENCES

Brunitzer, G., Best, J. S., Flamm, U. & Schrank, B. (1966). Zur phylogcnie des hämoglobins: Untorsuchugen am hämoglobin des kaninchens. Hoppe-Seyler's Zeitschrift für Physiologischc Chemie 347, 207.Google Scholar
Hunt, T., Hunter, T. & Munro, A. J. (1968). Control of haemoglobin synthesis: Distribution of ribosomos on the messenger RNA for α and β chains. Journal of Molecular Biology 36, 31.CrossRefGoogle ScholarPubMed
Rossi-Fakelli, A., Antonini, E. & Caputo, A. (1958). Studios on tho structure of haemoglobin. I. Physico-chemical properties of human globin. Biochemica et Biophysica Ada 30, 608.Google Scholar
Steele, P. R. M., Davies, J. D. & Graves, R. I. N. (1969 a). Some factors affecting the viability of freeze-thawed T4 bacteriophage. Journal of Hygiene 67, 107.CrossRefGoogle ScholarPubMed
Steele, P. R. M., Davies, J. D. & Greaves, R. I. N. (1969 b). Some factors affecting the viability of freeze-thawed T4 bactoriophago. II. Tho influenco of certain electrolytes on the degree of inactivation. Journal of Hygiene 67, 679.CrossRefGoogle Scholar
Tanford, C. (1968). Protein denaturation. Advances in Protein Chemistry 23, 122.Google ScholarPubMed
Von Eitrenstein, G. (1966). Translational variations in tho amino-acid sequence of the α-chain of rabbit haemoglobin. Cold Spring Harbor Symposia on Quantitative Biology 31, 705.CrossRefGoogle Scholar
Von Hippel, P. & Schleich, T. (1969). Ion effects on tho solution structure of macromolecules. Accounts of Chemical Research 2, 257.CrossRefGoogle Scholar
Waley, S. G. & Watson, J. (1953). Action of trypsin on polylysino. Biochemical Journal 55, 328.CrossRefGoogle Scholar