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lens culinaris/potássio
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6 resultados
Plant microbody proteins, I. Purification and characterization of catalase from leaves of lens culinaris.
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1) Catalase from green leaves of Lens culinaris (lentils) was investigated with respect to isoenzyme patterns. In contrast to other plants, which have been reported to contain multiple forms of catalase, only one form of this enzyme was revealed when crude extracts were subjected to starch gel
Differences in responses to iron deficiency between two legumes: lentil (Lens culinaris) and chickpea (Cicer arietinum).
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Two legumes, lentil and chickpea, were cultivated in nutrient solutions: Fe lacking or containing 30 microM Fe. After 12 days of Fe starvation, lentil showed a severe yellowing of young leaves, a large decrease in chlorophyll concentration, and a significant decline of plant biomass. Chickpea showed
The timing of cortical granule fusion, content dispersal, and endocytosis during fertilization of the hamster egg: an electrophysiological and histochemical study.
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To determine the temporal relationship between cortical granule exocytosis and the repetitive calcium transients, which are characteristic of mammalian fertilization, we monitored membrane addition from exocytosis during fertilization of hamster eggs. Continuous measurement of membrane capacitance
Interaction between calcofluor white and carbohydrates of alpha 1-acid glycoprotein.
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Interactions between the fluorescent probe, calcofluor white, and human serum albumin (HSA) and alpha 1-acid glycoprotein (orosomucoid) are compared. The two proteins have comparable isoelectric points, but alpha 1-acid glycoprotein is highly glycosylated (40% of glycans by weight), while the serum
Interaction between calcofluor white and carbohydrates of alpha 1-acid glycoprotein.
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Entrar Inscrever-se
Interactions between the fluorescent probe, calcofluor white, and human serum albumin (HSA) and alpha 1-acid glycoprotein (orosomucoid) are compared. The two proteins have comparable isoelectric points, but alpha 1-acid glycoprotein is highly glycosylated (40% of glycans by weight), while the serum
Localization of the lectin reactive sites in adult and prepubertal horse testes.
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The testes of prepubertal and adult horses were investigated using 10 horseradish peroxidase conjugated lectins combined with sialidase digestion and potassium hydroxide treatment, to localise the oligosaccharide sequences of glycoconjugates during spermatid maturation. In adult animals, the lectins
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