[Experimental study on in vivo erythrocyte labeling with 99m Tc using stannous chloride].
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Biomedical subjects
Publications and source records attributed to M Katayama.
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Four chromatographically different proteases were partially purified from defatted soybean flour, and their pH optima were around 5.0 to 5.6 using casein as the substrate. These soybean proteases were designated S1, S2, S3 and S4 according to their order of elution from a DEAE-cellulose column. Each gave a single peak of caseinolytic activity on a Sephadex G-200 column chromatogram, and corresponded to the molecular weights of about 50,000(S1), 35,000(S2), 60,000(S3) and 200,000(S4). The proteases could hydrolyze casein and poly-Glu. alpha-Casein was more rapidly hydrolyzed than beta-casein, but the esters or dipeptide could not be hydrolyzed. Aliquots of 10(-3) M Hg2+, Cu2+ and Zn2+ inhibited the caseinolytic activities by 70% to 90%, while other cations, Mn2+, Mg2+, Ca2+ and Ni2+, at the same concentration did not. SPI (10(-5) M) inhibited 80--90% of their activities, and EPNP (10(-5) M) inhibited their activities 30--60%, but DFP (10(-3) M), SSI (10(-3) M), PCMB (10(-4) M), NEM (10(-3) M) and EDTA (10(-3) M) were not inhibitory. The above results indicate that proteases S1, S2, S3 and S4 from defatted soybean flour can be classified as acid proteases.
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Green cells of Chlorella protothecoides grown in nitrogen-rich low glucose media may be reversibly transformed to entirely chlorophyll-less cells in low nitrogen high glucose media. Photosynthetic rates and fatty ester compositions were determined during light and dark bleaching and during greening. Linolenic acid content remained unchanged during greening or bleaching. During light greening chlorophyll content and photosynthetic activity increased while oleic acid content decreased dramatically. As a result, the percent composition of linolenate appeared to parallel photosynthetic capability. Implication of alpha-linolenate in oxygen production, therefore, can not be based upon fatty acid percentage composition data alone.
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Calcitonin gene-related peptide (CGRP) and substance P (SP) are released from sensory nerves upon exposure to irritating stimuli. Neutral endopeptidase (NEP), a membrane-bound peptidase, cleaves many peptides including SP, thereby limiting their biological actions. Recombinant NEP cleaved CGRP1 approximately 88-fold less rapidly than it cleaved SP. The slow cleavage by NEP of CGRP compared to SP suggests that this enzyme is likely to have weaker physiologic effects on CGRP than have been demonstrated for SP.