Tetraamido-substituted 2,3-naphthalocyanine zinc(II) complexes as phototherapeutic agents: synthesis, comparative photochemical and photobiological studies.

The aim of this study is to report the synthesis and photochemical and phototherapeutic activities of tetraamido-substituted 2,3-naphthalocyanine zinc(II) complexes (ZnNcs 5-8). Four naphthalocyanine complexes, tetrabenzamido- (ZnNc 5), tetramethoxybenzamido- (ZnNc 6), tetrahexylamido- (ZnNc 7) and tetradodecylamido- (ZnNc 8) naphthalocyanine zinc complexes absorbing at around 770 nm were synthesized. The dye-sensitized photo-oxidation of 1,3-diphenylisobenzofuran via 1O2 was studied in more detail in order to compare the quantum yields of these different sensitizers.

Hydrophobic Zn(II)-naphthalocyanines as photodynamic therapy agents for Lewis lung carcinoma.

Four Zn(II) 2,3-naphthalocyanines (unsubstituted ZnNc1, tetracetylamido substituted ZnNc2, tetramino substituted ZnNc3 and tetramethoxy substituted ZnNc4) incorporated into unilamellar liposomes of dipalmitoylphosphatidylcholine have been injected intra-peritoneally (i.p.) (0.

Chymotrypsin activation of melanosome tyrosinase in hamster melanotic melanoma.

The tyrosinase activity in two sucrose gradient isolated melanosome fractions from a melanotic hamster melanoma was found to increase after alpha-chymotrypsin treatment. The enhancement in tyrosinase activity had its maximum at a concentration of 1 mg/ml alpha-chymotrypsin after 120 min incubation at 37 degrees C. No direct activating effect of alpha-chymotrypsin was found either on the soluble tyrosinase fraction from freshly prepared untreaed whole-tumor homogenate or on purified mushroom tyrosinase.

[Ultrastructural changes in the liver of rats with a Yoshida tumor under exposure to cyclophosphamide].

Sixteen Wistar line rats with Joshida tumor were given cyclophosphamide either daily or with two-day intervals. The changes observed were mostly those related with the Golgi complex apparatus, lysosomes, biliary canaliculi as well as hyaloplasma. The degree of pronouncement of these changes was dependent on the duration of cyclophosphamide administration.

Cytochemical localization of peroxidase activity in normal, proliferating and neoplastic thyroid tissues of rats. An ultrastructural study.

In the control animals of thyroid peroxidase is localized within the membrane of rough endoplasmic reticulum, perinuclear cisternae, microvilli, lamellar structures of the GOLGI apparatus and dispersed through the cytoplasm small vesicles. 3 weeks treatment of the animals with MTU leads to disappearance of the peroxidase activity from the follicular cells. However, a prolongation of MTU administration until the 6th month and latter causes a reappearance of the peroxidase activity within the same structures of the proliferating cells as in the control animals.