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Amino acid sequence of normal (microheterogeneous) porcine immunoglobulin lambda chains
Biochemistry
|August 23, 1977
Summary
Researchers sequenced pig immunoglobulin lambda chains by using a novel fragmentation strategy. This method allowed for the complete determination of amino acid sequences in microheterogeneous proteins.
Area of Science:
- Immunology
- Protein Chemistry
- Biochemistry
Background:
- Previous studies determined partial amino acid sequences of pig immunoglobulin lambda chains.
- Microheterogeneity in protein sequences presents challenges for complete structural determination.
Purpose of the Study:
- To complete the major amino acid sequence of pig immunoglobulin lambda chains.
- To demonstrate a viable fragmentation strategy for sequencing microheterogeneous proteins.
Main Methods:
- Citraconylated pig lambda chains were digested with trypsin.
- Fragments were purified using gel filtration and ion-exchange chromatography.
- Intermediate-sized fragments enabled overlap information for sequence deduction.
Main Results:
- The complete amino acid sequence of pig immunoglobulin lambda chains was deduced.
- Amino acid compositions and partial sequences of selected fragments were analyzed.
- All 14 tryptic peptides were sequenced through overlap information.
Conclusions:
- A suitable fragmentation strategy can successfully sequence microheterogeneous proteins.
- This study provides the complete major amino acid sequence for pig immunoglobulin lambda chains.