Isolation,Purification and Sequence Analysis of a 24 kDa Protein from Luffa cylindrica Fruit Phloem Exudate
碩士 === 國立臺灣大學 === 植物學系 === 85 === AbstractP-proteins are groups of protein expressed specifically in the phloem. Their biological function have been not well defined so far. A polyclonal antibody against 24 kDa phloem protein was prepared i...
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| Format: | Others |
| Language: | zh-TW |
| Published: |
1997
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| Online Access: | http://ndltd.ncl.edu.tw/handle/02044158878502228750 |
| Summary: | 碩士 === 國立臺灣大學 === 植物學系 === 85 === AbstractP-proteins are groups of protein expressed specifically
in the phloem. Their biological function have been not well
defined so far. A polyclonal antibody against 24 kDa phloem
protein was prepared in our previous study. In the present
study, phloem proteins from Luffa cylindrica were separated with
SDS-PAGE and 2-D electrophoresis. There are four groups of
phloem protein in SDS-PAGE profile. A major band at 24 kDa and
some minor bands can be identified by the polyclonal antibody.
Most fruit phloem exudate protein are acidic in 2-D gel.
Immunoblotting study showed that 4-6 spots at 24 kDa with pI
ranging from 4 to 5.2 are detected. The antibody of pepo 24 kDa
also recognized the similar proteins expressed in a three-day-
old seedling and in xylem sap. A 24 kDa protein with pI 5.2
obtained from 2-D gel have 16 kinds of amino acids with high
contain of glycine (12.3%) aspartic acid(8.9%) and glutamic acid
(7.2%). The N-terminal sequencing is totally blocked. Further
cleavage of 24 kDa by CNBr was tested and peptide fragments were
transferred to VDF membrane for sequence analysis.
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