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The Complete Amino-Acid Sequence of Non-Immunolobulin Amyloid Fibril Protein AS in Rheumatoid Arthritis
- Source :
- European Journal of Biochemistry. 41:117-125
- Publication Year :
- 1974
- Publisher :
- Wiley, 1974.
-
Abstract
- The primary structure of a non-immunoglobulin amyloid protein AS has been determined. The protein was found to consist of 76 amino acid residues corresponding to a molecular weight of 9145. The sequence analysis showed clearly that the protein was homogeneous. A characteristic distribution of hydrophobic amino acids was observed and suggested as being of importance for the ability of this protein to form fibrils. A comparison of the protein with other amyloid protein AS showed a high degree of variability, particularly in the carboxyl-terminal region.
- Subjects :
- Amyloid
Chromatography, Paper
Carboxypeptidases
Fibril
Biochemistry
Arthritis, Rheumatoid
Chymotrypsin
Humans
Trypsin
Cyanogen Bromide
Amino Acids
Peptide sequence
chemistry.chemical_classification
biology
Chemistry
Protein primary structure
P3 peptide
Chromatography, Ion Exchange
Peptide Fragments
Amino acid
Molecular Weight
Amyloid A Protein
Liver
Chromatography, Gel
biology.protein
Spectrophotometry, Ultraviolet
Chromatography, Thin Layer
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 41
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....b29071bf63992f6390f467ce506ec583
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1974.tb03251.x