Rónai, A. Z.

Inhibition of neurotransmission by angiotensin I and II in rabbit isolated ear artery.

Eur J Pharmacol 179, 281-6.

Angiotensin I and II inhibited the nerve stimulation-induced pressure changes in isolated, perfused rabbit ear artery with an IC50 of 3.07 and 0.36 nM, respectively. Neither angiotensin I nor angiotensin II affected the basal pressure or the pressure changes elicited by exogenously administered norepinephrine (NE). The potency of angiotensin I was unaltered by 10(-5) M captopril, indicating that conversion by angiotensin converting enzyme (ACE) was not necessary and did not take place. [Sar1,Val5,Ala8]angiotensin II (3 x 10(-8) M) antagonized the effect of angiotensin I. These findings could have implications regarding ACE inhibitor therapy and the pathophysiology of migraine.

Nyitray, L. , Goodwin, E. B. & Szent-Györgyi, A. G.

Nucleotide sequence of full length cDNA for a scallop striated muscle myosin heavy chain.

Nucleic Acids Res 18, 7158.

Kwon, H., Goodwin, E. B., Nyitray, L. , Berliner, E., O'Neall-Hennessey, E., Melandri, F. D. & Szent-Györgyi, A. G.

Isolation of the regulatory domain of scallop myosin: role of the essential light chain in calcium binding.

Proc Natl Acad Sci U S A 87, 4771-5.

Hollósi, M., Süli-Vargha, H., Medzihradszky, K., Fasman, G. D., Kunos, G. & Gráf, L.

Structural determinants of the binding of gliadin fragments to human peripheral blood lymphocytes.

Neuropeptides 17, 111-6.

A series of alpha-gliadin fragments, structurally related to alpha-gliadin-(43-49), were synthesized. The effect of these fragments and beta-casomorphin and naloxone on the steady-state binding of [125I]-alpha-gliadin-(43-49) to human peripheral blood lymphocytes was investigated. In an attempt to correlate the binding data with the conformation of the peptides, their circular dichroism spectra were measured in both trifluorethanol and aqueous solution. It was found that there is a striking correlation between the results of the binding studies and the chiroptical properties of the gliadin fragments. The presence of N-terminal tyrosine and the tendency of the peptides to adopt periodic, 310 helix-like secondary structure appear to be crucial for the binding to human peripheral blood lymphocytes.