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vriesea incurvata/urea
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High-molecular-weight serine proteinase from lobster muscle that degrades myofibrillar proteins.
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A latent alkaline serine proteinase (ASP) has been extracted from the soluble fraction of lobster claw and abdominal muscles. The enzyme, which was irreversibly activated 30- to 40-fold by brief (2-3 min) heating at 60 degrees C, had an optimal caseinolytic activity at pH 7.75. Its molecular weight
Involvement of aquaporins on nitrogen-acquisition strategies of juvenile and adult plants of an epiphytic tank-forming bromeliad.
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Depending on the N source and plant ontogenetic state, the epiphytic tank-forming bromeliad Vriesea gigantea can modulate aquaporin expression to maximize the absorption of the most available nitrogen source. Epiphytic bromeliads frequently present a structure formed by the overlapping of leaf bases
Detection of urease in the cell wall and membranes from leaf tissues of bromeliad species.
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Urea is an important nitrogen source for some bromeliad species, and in nature it is derived from the excretion of amphibians, which visit or live inside the tank water. Its assimilation is dependent on the hydrolysis by urease (EC: 3.5.1.5), and although this enzyme has been extensively studied to
Nitrogen metabolism in leaves of a tank epiphytic bromeliad: characterization of a spatial and functional division.
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The leaf is considered the most important vegetative organ of tank epiphytic bromeliads due to its ability to absorb and assimilate nutrients. However, little is known about the physiological characteristics of nutrient uptake and assimilation. In order to better understand the mechanisms utilized
Microbial activities and foliar uptake of nitrogen in the epiphytic bromeliad Vriesea gigantea.
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In contrast to terrestrial plants, epiphytic tank bromeliads take up nutrients mainly over their tank leaf surface. The form in which nutrients are available in the tanks is determined by the source and the complex interplay between tank microbes, which transform them and the epiphytes that take
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