Characterization of the Protease Processing Sites in a Multidomain Proteinase Inhibitor Precursor from Nicotiana Alata

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Characterization of the Protease Processing Sites in a Multidomain Proteinase Inhibitor Precursor from Nicotiana Alata

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im Mai 1995 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в травні 1995

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Characterization of the Protea ...... Precursor from Nicotiana Alata

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Characterization of the Protea ...... Precursor from Nicotiana Alata

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Characterization of the Protea ...... Precursor from Nicotiana Alata

@en

Characterization of the Protea ...... Precursor from Nicotiana Alata

@nl

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Characterization of the Protea ...... Precursor from Nicotiana Alata

@en

Characterization of the Protea ...... Precursor from Nicotiana Alata

@nl

P1476

Characterization of the Protea ...... Precursor from Nicotiana Alata

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P2093

Gavin E. Reid

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Guan Lim

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Marilyn A. Anderson

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Peter A. Barton

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Robyn L. Heath

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P2860

Protein inhibitors of proteinases

Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors.

Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains.

The complete amino acid sequence and the trypsin reactive (inhibitory) site of the major proteinase inhibitor from the fruits of aubergine (Solanum melongena L.).

Sequence variability of three alleles of the self-incompatibility gene of Nicotiana alata.

A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms.

Vesicle transport and processing of the precursor to 2S albumin in pumpkin.

P304

250-257

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P31

scholarly article

P356

10.1111/J.1432-1033.1995.0250I.X

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P407

English

P433

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P478

230

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P50

Richard Simpson

P577

1995-05-01T00:00:00Z

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P921

cell biology

molecular biology