The Amino Acid Sequence of Kunitz type Soybean Trypsin Inhibitor, Ti d,Derived from Its Nucleotide Sequence and Its Comparison with Ti a
XIN Hua,CAO Kaiming,XIE Kefang,GU Qimin
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(Department of Biochemistry,Fudan University,Shanghai 200433
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1999-08-20
1999-08-20
1999-08-20
发布日期
1999-08-20
Abstract
It was widely thought that 3 variants of Kunitz type trypsin inhibitor(SBTi A 2) existed in soybean seed storage protein.Three of codominant alleles Ti a,Ti b and Ti c were identified to decode these SBTi A 2 inhibitors and the amino acid sequences of them were determined,of which one or more different amino acid were found.Ti d was a new variant allele of SBTi A 2 discovered after analyzing more than 15 000 samples of soybean seed in China.In order to study the structure features of Ti d protein,the amino acid sequence of this protein was deduced from its coding region which was amplified by PCR from soybean genomic DNA and sequenced.By comparison with Ti a protein,two different amino acid residue were found between Ti a and Ti d proteins.One was an extra Ala inserted in the signal peptide of Ti d,with 8 residues from N terminal,and the other existed in the mature protein,with Glu 69 in Ti a protein turned into Lys 69 in Ti d protein.The amino acid sequence of Ti d mature protein was also different from those of Ti a and Ti b.
XIN Hua,CAO Kaiming,XIE Kefang,GU Qimin.
The Amino Acid Sequence of Kunitz type Soybean Trypsin Inhibitor, Ti d,Derived from Its Nucleotide Sequence and Its Comparison with Ti a[J]. Chinese Journal of Biochemistry and Molecular Biology, 1999, 15(04): 671-673
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