The complete amino acid sequence of human C-reactive protein has been established. Distant homologies to C3 homology region in the CH2 domain of IgG and to C3a anaphylotoxin have been noted. No homology to other immunoglobulin homology regions or to the same homology region in other heavy chains was observed. The previously reported homologies between rabbit and human C-reactive protein and pro...

We have determined the nucleotide sequence coding for the chicken brain a-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The a-chain of brain spectrin contains 22 segments of which 20 corr...

The complete amino acid sequence of pig liver thioltransferase has been determined. The homogeneous protein was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The resulting peptides were purified by reversed-phase high performance liquid chromatography and ion-exchange fast protein liquid chromatography. Sequencing of the fragments was achieved with e...

Apolipoprotein-serine (apoLP-Ser or apoC-I) is one of the apoprotein constituents of human plasma very low density lipoprotein. The protein has 57 amino acid residues, including one residue of methionine and is lacking histidine, cysteine, cystine, and tyrosine. The NH2 terminus of apoLP-Ser is threonine and the COOH terminus is serine. Cleavage of apoLP-Ser with cyanogen bromide, followed by c...

Human placental triosephosphate isomerase was isolated by an improved procedure and recovered with the highest specific activity ever reported. Employing this purification procedure, sufficient amounts of the enzyme were obtained for detailed primary structural studies. For sequences analysis, the enzyme was reduced and carboxymethylated and subjected to tryptic and chymotryptic digestions. The...

The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residu...

Single-chain pro-urokinase is an inactive proenzyme form of human urokinase with a single-chain structure and a Mr of 50,000 and converted to the active two-chain form by catalytic amounts of plasmin. It was isolated from culture fluid of human kidney cells and subjected to chemical (CNBr) and proteolytic (lysyl endopeptidase) degradation. The resulting peptides were separated by reverse-phase ...

Parathymosin has been isolated from rat thymus and from rat liver. Its primary structure is reported as follows: (Sequence; see text). The blocking group at the NH2 terminus was identified by mass spectrometry as acetyl. Regions homologous to amino acid sequences in prothymosin alpha were found to be located between residues 14-20, 23-25, 33-39, 41-43, and 83-87 of parathymosin.

The complete amino acid sequence of human neutrophil elastase has been determined. The protein consists of 218 amino acid residues, contains two asparagine-linked carbohydrate side chains, and is joined together by four disulfide bonds. Comparison of the sequence to other serine proteinases indicates only moderate homology with porcine pancreatic elastase (43.0%) or neutrophil cathepsin G (37.2...

MOTIVATION An ambitious goal of proteomics is to elucidate the structure, interactions and functions of all proteins within cells and organisms. The expectation is that this will provide a fuller appreciation of cellular processes and networks at the protein level, ultimately leading to a better understanding of disease mechanisms and suggesting new means for intervention. This paper addresses ...