Zobrazeno 1 - 10
of 59
pro vyhledávání: '"V A, Najjar"'
Autor:
V A, NAJJAR, L E, HOLT
Publikováno v:
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.). 61
Autor:
V A, NAJJAR
Publikováno v:
The interne. 12
Autor:
V A, NAJJAR, C C, DEAL
Publikováno v:
Bulletin of the Johns Hopkins Hospital. 80(3)
Autor:
V A, NAJJAR, I M, RATCLIFFE
Publikováno v:
Bulletin of the Johns Hopkins Hospital. 80(2)
Autor:
V. A. Najjar
Publikováno v:
Klinische Wochenschrift. 57:751-756
The tetrapeptide tuftsin (Thr-Lys-Pro-Arg) stimulates phagocytosis by blood neutrophilic granulocytes and tissue macrophages in a highly specific manner. Tuftsin is cleaved off the carrier γ-globulin molecule as the free active form by two enzymes.
Autor:
V A Najjar, P P Layne
Publikováno v:
Journal of Biological Chemistry. 250:966-972
The phosphoryl group on the serine residue at the active site of phosphoglucomutase is presumed to undergo nucleophilic attack by the monophosphate substrates glucose 1- and glucose 6-phosphate to form glucose 1,6-diphosphate. Fluoride, hydroxylamine
Autor:
B. V. Fidalgo, V. A. Najjar
Publikováno v:
Biochemistry. 6:3386-3392
Publikováno v:
Proceedings of the National Academy of Sciences. 57:665-672
In the interest of clear presentation, it is appropriate and perhaps necessary to outline the sequence of the various findings that gave rise to the concept of the physiological function of 'y-globulin and led to the present work. Studies on the mech
Autor:
R. B. Merrifield, V. A. Najjar
Publikováno v:
Biochemistry. 5:3765-3770
Autor:
P P, Layne, V A, Najjar
Publikováno v:
The Journal of biological chemistry. 250(3)
The phosphoryl group on the serine residue at the active site of phosphoglucomutase is presumed to undergo nucleophilic attack by the monophosphate substrates glucose 1- and glucose 6-phosphate to form glucose 1,6-diphosphate. Fluoride, hydroxylamine