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Purification and characterization of phytocystatins from kiwifruit cortex and seeds
Rassam, M ; Laing, W.A
Phytochemistry (Oxford), 2004, Vol.65 (1), p.19-30
[Periódico revisado por pares]
Amsterdam: Elsevier
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Título:
Purification and characterization of phytocystatins from kiwifruit cortex and seeds
Autor:
Rassam, M
;
Laing, W.A
Assuntos:
actinidain
;
Actinidia - chemistry
;
Actinidia deliciosa
;
Actinidiaceae
;
Amino Acid Sequence
;
amino acid sequences
;
apples
;
Arabidopsis thaliana
;
Biological and medical sciences
;
Chromatography, High Pressure Liquid - methods
;
Cluster Analysis
;
complementary DNA
;
consensus sequence
;
cortex
;
cystatins
;
Cystatins - genetics
;
Cystatins - isolation & purification
;
Cystatins - pharmacology
;
Cysteine Endopeptidases - metabolism
;
cysteine proteinase inhibitors
;
Cysteine Proteinase Inhibitors - isolation & purification
;
Cysteine Proteinase Inhibitors - pharmacology
;
cysteine proteinases
;
Dermatophagoides pteronyssinus
;
enzyme inhibition
;
enzyme substrates
;
Enzymes
;
Ericales
;
expressed sequence tags
;
Fruit - chemistry
;
fruit crops
;
fruits (plant anatomy)
;
Fundamental and applied biological sciences. Psychology
;
Humans
;
kiwifruit
;
Malus domestica
;
matrix-assisted laser desorption-ionization mass spectrometry
;
Metabolism
;
Molecular Sequence Data
;
phylogeny
;
plant extracts
;
Plant physiology and development
;
plant proteins
;
proteinase inhibitors
;
purification
;
seeds
;
Seeds - chemistry
;
Sequence Alignment
;
Sequence Homology, Amino Acid
;
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
É parte de:
Phytochemistry (Oxford), 2004, Vol.65 (1), p.19-30
Notas:
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição:
Kiwifruit cysteine proteinase inhibitors (KCPIs) were purified from the cortex and seeds of kiwifruit after inactivation of the abundant cortex cysteine proteinase actinidain. One major (KCPI1) and four minor cystatins were identified from Actinidia deliciosa ripe mature kiwifruit cortex as well as a seed KCPI from A. chinensis. The predominant cortex cystatin, KCPI1, inhibited clan CA, family C1 (papain family) cysteine proteinases (papain, chymopapain, bromelain, ficin, human cathepsins B, H and L, actinidain and the house dust mite endopeptidase 1), while cysteine proteinases belonging to other families, [clostripain (C11), streptopain (C10) and calpain (C2)] were not inhibited. Inhibition constants (K(I)) ranged between 0.001 nM for cathepsin L and 0.98 nM for endopeptidase 1. The K(I) (14 nM) for KCPI1 inhibiting actinidain is at least 2 orders of magnitude higher than for other plant proteinases measured. The cortex KCPI1 and a seed KCPI purified from seeds had the same N-terminal sequence (VAAGGWR-PIESLNSAEVQDV). BLAST-matching the peptide sequence against an in-house generated Actinidia EST database, identified 81 cDNAs that exactly matched the measured KCPI1 peptide sequence. Peptide sequences of two other cortex KCPIs each exactly matched a predicted peptide sequence of a cDNA from kiwifruit. The predicted peptide sequence of KCPI1 of 116 amino acids encodes a signal peptide and does not contain cysteine. Without the signal peptide (mature protein), KCPI1 has a molecular mass of approximately 11 kDa, possesses the consensus sequence characteristic for the phytocystatins and shows the highest homology to a cystatin from Citrusxparadisi (52% identity). This is the first report of phytocystatins from the Ericales.
Editor:
Amsterdam: Elsevier
Idioma:
Inglês
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