Reinigung der Proteinase aus Nepenthes-Kannensaft

Steckelberg, Rosa Maria de Brito; Lüttge, Ulrich; Weigl, Josef

doi:10.1007/bf00409815

Cited by 17 publications

(9 citation statements)

References 3 publications

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“…Moreover, tests with silver nitrate showed Cl-to be present in the secretions of many pitchers. Recently, Nakayma and Amagase [2] described the partial purification of the acid protease from opened pitchers and in contrast with the results of earlier authors [3,4] and ours [ 1 ] , the Japanese workers could not find any proteolytic activity in the secretions of unopened pitchers. Thus, they could not exclude the bacterial origin of their protease.…”

Section: Resultscontrasting

confidence: 89%

Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin

Jentsch

1972

FEBS Letters

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Section: Resultscontrasting

confidence: 89%

Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin

Jentsch

1972

FEBS Letters

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“…At present, the role of acidi®cation of pitcher¯uid may be deduced as follows. The optimum pH of proteolytic enzymes is around pH 2±3 (Steckelberg et al 1967;Nakayama and Amagase 1968;Athauda et al 1998), and such a low pH should be favorable to the digestive enzymes in the pitcher¯uid. Higashi et al (1993) previously reported that 26 strains of bacteria were isolated from Nepenthes pitchers and that 10 of the 26 strains had casein hydrolase activity.…”

Section: Eect Of Proton Pump Modulatorsmentioning

confidence: 99%

“…These ®ndings suggest that the acidity of pitcher¯uid is due to HCl. The acidi®cation of pitcher¯uid is thought to play an important role in digestion and absorption of prey based on the following facts: (i) the pH of pitcher¯uid is reduced when prey accumulates in the¯uid (LuÈ ttge 1964), (ii) the optimum pH of proteolytic enzyme in pitcher¯uid is around pH 2±3 (Steckelberg et al 1967;Nakayama and Amagase 1968;Athauda et al 1998), and (iii) proton gradients across the plasma membrane are generally used to drive uptake of many solutes (ions, metabolites, etc.) (Michelet and Boutry 1995).…”

Section: Introductionmentioning

confidence: 99%

Plasma-membrane H + -ATPases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco

Fukusaki

Kobayashi

2001

Planta

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Nepenthes is a unique genus of carnivorous plants that can capture insects in trapping organs called pitchers and digest them in pitcher fluid. The pitcher fluid includes digestive enzymes and is strongly acidic. We found that the fluid pH decreased when prey accumulates in the pitcher fluid of Nepenthes alata. The pH decrease may be important for prey digestion and the absorption of prey-derived nutrients. To identify the proton pump involved in the acidification of pitcher fluid, plant proton-pump homologs were cloned and their expressions were examined. In the lower part of pitchers with natural prey, expression of one putative plasma-membrane (PM) H+-ATPase gene, NaPHA3, was considerably higher than that of the putative vacuolar H+-ATPase (subunit A) gene, NaVHA1, or the putative vacuolar H+-pyrophosphatase gene, NaV-HP1. Expression of one PM H+-ATPase gene, Na-PHA1, was detected in the head cells of digestive glands in the lower part of pitchers, where proton extrusion may occur. Involvement of the PM H+-ATPase in the acidification of pitcher fluid was also supported by experiments with proton-pump modulators; vanadate inhibited proton extrusion from the inner surface of pitchers, whereas bafilomycin A1 did not, and fusicoccin induced proton extrusion. These results strongly suggest that the PM H+-ATPase is responsible for acidification of the pitcher fluid of Nepenthes.

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“…Considering the presence of protease in the pitcher fluid, insect proteins should be an important nitrogen source for Nepenthes. To date, proteases have been purified and characterized from sterile pitcher fluids of several species of Nepenthes (Steckelberg et al 1967;Jentsch 1972;To¨ke´s et al 1974). These studies provide evidence that aspartic proteinases (APs) are secreted into the pitcher.…”

Section: Introductionmentioning

confidence: 98%

Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco

Fukusaki

Kobayashi

2002

Planta

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Carnivorous plants acquire significant amounts of nitrogen from insects. The tropical carnivorous plant Nepenthes accumulates acidic fluid containing aspartic proteinase (AP) in its trapping organs (pitchers), suggesting that the plant utilizes insect protein as a nitrogen source. Aspartic proteinases have been purified and characterized from sterile pitcher fluid of several species of Nepenthes; however, there is, as of yet, no information about sequence and expression of Nepenthes AP genes. To identify the pitcher AP, we cloned plant AP homologs from N. alata and examined their expressions. Five AP homologs ( NaAP1-NaAP5) were obtained by reverse transcription-polymerase chain reaction with degenerate primers designed for the conserved sequences of plant APs. Alignment of deduced amino acid sequences with other plant APs demonstrated that NaAP1-NaAP4 contained a plant-specific insert (PSI), a unique sequence of plant AP. However, NaAP5 did not possess the insert, and had a shorter sequence (by >100 amino acids) than the other APs. Northern analysis using a part of the coding region of NaAP1 as a probe showed that bands of approx. 1.8 kb corresponding to the sizes of NaAP1-NaAP4 mRNA were present in roots, stems, leaves, tendrils, and lower part of the pitchers, but a band of approx. 1.3 kb corresponding to the size of NaAP5 mRNA was not observed in any organs. In pitchers, highest expressions of NaAP1-NaAP4 were seen in the lower part of open pitchers containing natural prey, suggesting that the expressions of NaAP1-NaAP4 are coupled with prey capture. Transcripts of NaAP2 and NaAP4 were detected in the digestive glands, where AP secretion may occur. This result suggests that NaAP2 and NaAP4 are the possible APs secreted into the pitcher of N. alata.

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Reinigung der Proteinase aus Nepenthes-Kannensaft

Abstract: The proteolytic enzymes from the sterile secretion of the pitchers of 3 Nepenthes species were purified to electrophoretic homogenity by chromatography on Ecteola cellulose. The properties of the purified enzymes were investigated.

Cited by 17 publications

References 3 publications

Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin

Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin

Plasma-membrane H + -ATPases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco

Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco

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