Van Dyke protein

The analogs discussed so far reveal certain features of the various oxytocin receptors. The molecule binds, however, not merely to the receptors in the target organs, but also to a carrier protein, originally known as the van Dyke protein [54] that was renamed neurophysin after its isolation in pure form. It is rather remarkable that for binding of oxytocin to this protein the free N-terminal amino group, which is not needed for activity, is quite essential [55]. 

In this and other respects e.g histidine was absent, it was different from the so-called van Dyke protein. We decided to call the major sub-fraction neurophysin-M until more was known about it and a better name could be found. Neurophysin-M behaved as a homogeneous protein in the ultracentrifuge and assuming a partial specific volume of 0.7 9 ml. per g. a molecular weight of 23 000 was calculated. During the course of the work we began to study the electrophoretic behaviour of the proteins in the buffer devised by Ferguson and Wallace In this system neurophysin-M... 

Van Dyke has isolated a protein from the neurohypophysis that possesses the activity of both ocytocin and vasopressin (the Van Dyke protein ). By suitable physical methods, ocytocin and vasopressin can be liberated from the protein. The protein may be considered a storage and transport form of the low molecular... 

Zelisko, P. Bartzoka, V. Brook, M. A. Exploiting Favorable Silicone-Protein Interactions Stabilization Against Denaturation at Oil-Water Interfaces. In Synthesis and Properties of Silicones and Silicone-Modified Materials Clarson, S. J., Fitzgerald, J. J., Owen, M. J., Smith, S. D., Van Dyke, M. E., Eds. ACS Symposium Series 838 American Chemical Society Washington, DC, 2003 pp 212-221. 

Lupas, A., Van Dyke, S., and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164. 

Amino acids in posterior pituitary protein. Nature, 165, 975 (1950). With H. B. van Dyke. 

Shapira, L., Takashiha, S., Champagne, C., Amar, S., and Van Dyke, T.E. (1994). Involvement of protein kinase C and protein tyrosine kinase in hpopolysaccharide-induced TNF-alpha and IL-1 heta production by human monoc3des. J Immunol 153, 1818-24. 

Shapira, L., Sylvia, V.L., Halahi, A., Soskolne, W.A., Van Dyke, T.E., Dean, D.D., Boyan, B.D., and Schwartz, Z. (1997). Bacterial hpopolysaccharide induces early and late activation of protein kinase C in inflammatory macrophages by selective activation of PKC-epsilon. Biochem Biophys Res Commun 240, 629-34. 

H.B. van Dyke, B.F. Chow, R.O. Creep, A. Rothen, Isolation of a protein from the pars neuralis of the ox pituitary with constant oxytodc, pressor and diuresis inhibiting activities. J. Pharmacol. Exper. Therap. 74 190-209 (1942)... 

Xaylor, M. D. Van Dyke, K. Bowman, L. L. Miles, P. R. Hubbs, A. R Mason, R. J. Shannon, K. Reasor, M. J. A characterization of amiodarone-induced pulmonary toxicity in R344 rats and identification of surfactant protein-D as a potential biomarker for the development of the toxicity. Toxicol. Appl. Pharmacol. 2000,167,182-190. 

The active polypeptides in the secretory granules are probably not present in a free form. Van Dyke has isolated a protein called neurofisin (mol wt 30,000), which apparently binds 1 molecule of vasopressin and 1 molecule of oxytocin. The nature of the bond between the active hormone and the supporting protein is unknown. 

Butyl alcohols solubilize the ocytocic substances only from extracts treated with acids at a pH close to 3.9, at which pH proteins precipitate. The same phenomenon is true of hog pituitary. This behavior is due to the ocytocin-protein-complex which may represent the mother molecule of Van Dyke. 

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