Serum and amniotic fluid mucoproteins in normal and toxaemic pregnancy

Mukherjee, Gourab; Sharma, Damyanti; Shanker, Vicki; Lai, Hollie

doi:10.1007/bf02867846

Cited by 2 publications

(3 citation statements)

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“…Construction of cDNA library. Starting with 5 g leaves, total cellular RNA was prepared from M. pudica fresh leaves by a phenol/SDS method [11]. Poly(A)-rich RNA was isolated from total cellular RNA using an oligo(dT)-cellulose column supplied in the mRNA purification kit.…”

Section: Methodsmentioning

confidence: 99%

“…Purification of the expressed protein from cloned gene. The recombinant apyrase from E. coli was purified by a protocol similar to that for the plant enzyme [11]. Native gel electrophoresis was carried out with crude cell lysate followed by activity staining with ATP.…”

Section: Methodsmentioning

confidence: 99%

“…of the M. pudica leaf to external stimuli such as touch [10,11]. Further characterization of the apyrase showed that it is a complex of polypeptide and polysaccharide and that this complex formation is mediated through Ca 2ϩ .…”

mentioning

confidence: 99%

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An apyrase from Mimosa pudica contains N5,N10‐methenyl tetrahydrofolate and is stimulated by light

Ghosh

Biswas

Roy

1998

European Journal of Biochemistry

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An apyrase (NTP/NDPase) implicated in the response of Mimosa pudica to stimuli, such as touch, has been cloned, sequenced and expressed in Escherichia coli. While purifying and characterizing this enzyme, it was observed that a chromophore is associated with it, having absorption in the ultraviolet-A/ blue region of the spectrum. The absorbance maximum of the chromophore, purified from the enzyme complex by gel filtration and HPLC, is around 350 nm. The chromophore has been identified as N5,N10-methenyl tetrahydrofolate (MTHF) by comparing the excitation and emission spectra of synthetic MTHF and the isolated cofactor, and by reconstitution of the enzyme complex with synthetic MTHF. Upon excitation with light (350 nm), an increase of apyrase activity was observed in the purified or reconstituted holoenzyme but not in the apoenzyme. The wavelength dependence of the light stimulation matched well with the fluorescence excitation spectra of the cofactor, MTHF. Possible implications of the results for signal transduction in M. pudica have been discussed.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%