Zobrazeno 1 - 10
of 111
pro vyhledávání: '"M. Zaoral"'
Publikováno v:
Journal of Peptide Science. 6:123-129
Two cyclic disulfides of structure tsqb">Cys-Tyr-Arg-Arg-Tyr-Cys-NH2 (1) and tsqb">Cys-Tyr(Me)-Arg-Arg-Tyr(Me)-Cys-NH2 (2), two nonapeptide derivatives of 1 extended at the C-terminal with Pro-Arg-Gly-NH2 (3) or Pro-D-Arg-Gly-NH2 (4) and derivatives
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 6(3)
Two cyclic disulfides of structure Cys-Tyr-Arg-Arg-Tyr-Cys-NH2 (1) and Cys-Tyr(Me)-Arg-Arg-Tyr(Me)-Cys-NH2 (2), two nonapeptide derivatives of 1 extended at the C-terminal with Pro-Arg-Gly-NH2 (3) or Pro-D-Arg-Gly-NH2 (4) and derivatives of 3 and 4 h
Autor:
M. Zaoral
Publikováno v:
ChemInform. 21
Publikováno v:
Pathobiology. 53:260-264
Each of a series of synthetic peptidoglycan subunits and subunit analogues was injected in combination with streptococcus type M24 antigen extract. The substances tested were: (8a) N-acetylmuramyldipeptide (MDP) and the following derivatives thereof:
Publikováno v:
Pathobiology. 51:29-38
A series of synthetic subunits and analogues of streptococcal peptidoglycan was prepared and used in fever and tolerance experiments on rabbits. The lengthening of the chain of the peptide moiety of peptidoglycan did not result in pyrogenic activity,
Publikováno v:
Pathobiology. 47:258-268
The ability of some synthetically prepared analogues of Streptococcus peptidoglycan subunits (dipeptide, tetrapeptide, glycodipeptide and glycotetrapeptide) to cause fever in rabbits and lysis of rabbit blood platelets was studied. While di- and tetr
Publikováno v:
Collection of Czechoslovak Chemical Communications. 30:2812-2816
Publikováno v:
Collection of Czechoslovak Chemical Communications. 31:90-97
Autor:
M. Zaoral
Publikováno v:
Collection of Czechoslovak Chemical Communications. 30:1853-1868
Publikováno v:
The Lancet. 291:948-952
A synthetic analogue of vasopressin, in which the L-arginine in position 8 has been replaced by D-arginine and the free amino group in position 1 has been removed by replacing the hemicystine component at position 1 by β-mercaptopropionic acid, has