Immunotherapy with GcMAF revisited - A critical overview of the research of Nobuto Yamamoto.

This overview describes the research of Nobutu Yamamoto (Philadelphia) concerning immunotherapy with GcMAF for patients with cancer and for patients infected with pathogenic envelope viruses. GcMAF (Group-specific component Macrophage-Activating Factor) is a mammalian protein with an incredible potency to directly activate macrophages. Since the late 1980s Yamamoto's investigations were published in numerous journals but in order to understand the details of his research, a minute survey of many of his patents was required.

Multiple -glycosidases in human serum as detected with the substrate DNP-α-GalNAc. II. Three α--acetylgalactosaminidase-like activities in the pH 5 to 8 region.

With the substrate DNP-α-GalNAc (2,4-dinitrophenyl--acetyl-α-d-galactosaminide) three α--acetylgalactosaminidase-like activities could be distinguished in serum, in addition to the classical lysosomal enzyme (Naga, EC 3.2.1.

Multiple -glycosidases in human serum as detected with the substrate DNP-α-GalNAc. I. A new assay for lysosomal α--acetylgalactosaminidase.

This paper presents a new assay to determine the activity of the lysosomal enzyme α--acetylgalactosaminidase (Naga, EC 3.2.1.

Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H₂O₂--implications for their role in disease, especially cancer.

Mammalian NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial inner membrane catalyzes the oxidation of NADH in the matrix. Excess NADH reduces nine of the ten prosthetic groups of the enzyme in bovine-heart submitochondrial particles with a rate of at least 3,300 s⁻¹. This results in an overall NADH→O₂ rate of ca.

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: II. Comparison of the proposed working hypothesis with literature data.

The first purification of bovine NADH:ubiquinone oxidoreductase (Complex I) was reported nearly half a century ago (Hatefi et al. J Biol Chem 237:1676-1680, 1962). The pathway of electron-transfer through the enzyme is still under debate.