scholarly journals Immunoglobulin λ-chains. The complete amino acid sequence of a Bence-Jones protein

1968 ◽  
Vol 110 (4) ◽  
pp. 631-652 ◽  
Author(s):  
C. Milstein ◽  
J. B. Clegg ◽  
J. M. Jarvis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Total Amino Acid ◽  
Cysteine Residues ◽  
Bence Jones Protein ◽  
Chromatographic Techniques ◽  
Peptic Digestion ◽  
Similarities And Differences ◽  
Methionine Residues ◽  
Bence Jones Proteins

The total amino acid sequence of a λ Bence-Jones protein has been established. The protein contains 211 residues, which include two methionine residues. Splitting with cyanogen bromide gave three fragments, the largest of which included the C-terminal half, which is common to other Bence-Jones proteins of the same type. The peptides obtained by tryptic, chymotryptic and peptic digestion were isolated and purified by paper-electrophoretic and chromatographic techniques. Reduction followed by carboxymethylation of the cysteine residues with radioactive iodoacetate was found to be a powerful tool in the isolation of some insoluble peptides. Unusual features of the molecule are the fact that it contains six cysteine residues and not five as observed in both κ and λ Bence-Jones proteins studied previously, and its size, which seems two residues smaller than the smallest Bence-Jones protein studied hitherto. The similarities and differences between this and other Bence-Jones proteins are discussed.

Disulfide bonds of basic acrosin inhibitor (BUSI II) from bull seminal plasma

1984 ◽  
Vol 49 (5) ◽  
pp. 1204-1210 ◽  
Author(s):  
Alena Rzavská ◽  
Bedřich Meloun ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Disulfide Bonds ◽  
Cysteine Residues ◽  
Chromatographic Techniques

The thermolysin digest of the basic acrosin inhibitor (molecular weight 6 200) was resolved on a column of Sephadex G-15 and subsequently by electrophoretic and chromatographic techniques. Cysteine peptides, which link together half-cysteine residues 7 and 39, 17 and 36, and 25 and 57 by disulfide bonds, were isolated. The structure of the molecule of the basic acrosin inhibitor corresponds to structures of inhibitors of the Kazal type. The amino acid sequence of a few residues in the basic acrosin inhibitor has been revised.

scholarly journals A STUDY OF IMMUNOGLOBULIN STRUCTURE

1966 ◽  
Vol 124 (3) ◽  
pp. 307-330 ◽  
Author(s):  
C. Baglioni ◽  
D. Cioli
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Mapping ◽  
Gel Filtration ◽  
Bence Jones Protein ◽  
Type K ◽  
The Common ◽  
L Proteins ◽  
Peptide Maps ◽  
Bence Jones Proteins

Urinary proteins of patients with myeloma, prepared by precipitation with ammonium sulphate, have been separated by gel filtration on Sephadex G-100 after reduction and aminoethylation. Many specimens separated into a major peak of Bence Jones protein and into minor peaks of albumin, a protein tentatively identified with heavy chain and a smaller molecular weight protein corresponding to the variable portion of the corresponding Bence Jones protein. The Bence Jones protein purified by gel filtration was analyzed by electrophoresis and by peptide mapping after tryptic digestion. The peptide maps of 24 type K and 20 type L Bence Jones proteins were compared. A set of common peptides was identified in the peptide maps of the Bence Jones proteins of the same type; the common peptides of type K proteins were completely different from the common peptides of type L proteins. The patterns of distinctive peptides was compared; no similarities were found between distinctive peptides of type K and of type L proteins. Some similarities were observed in the distinctive peptides of proteins of the same type. The similarities involved in many cases peptides containing cysteine, whereas similarities in other peptides were limited. This observation suggested that the amino acid sequence around the cysteines of the variable NH2-terminal half of the Bence Jones proteins may show less variability than other sequences. A few proteins of the same type differed in all their distinctive peptides, an indication that multiple amino acid differences exist between individual Bence Jones proteins. The genetic mechanisms responsible for the variability in the amino acid sequence of the NH2-terminal half of the light chains of immunoglobulins are discussed in view of the results of the comparison by peptide mapping of the Bence Jones proteins.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

scholarly journals The Amino Acid Sequence of a κ Type Bence-Jones Protein

1969 ◽  
Vol 244 (13) ◽  
pp. 3537-3549 ◽  
Author(s):  
E J Whitley ◽  
K Titani ◽  
F W Putnam
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bence Jones Protein

scholarly journals The Amino Acid Sequence of a κ Type Bence-Jones Protein

1969 ◽  
Vol 244 (13) ◽  
pp. 3521-3536 ◽  
Author(s):  
K Titani ◽  
E J Whitley ◽  
F W Putnam
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bence Jones Protein

scholarly journals The Amino Acid Sequence of a κ Type Bence-Jones Protein

1969 ◽  
Vol 244 (13) ◽  
pp. 3550-3560 ◽  
Author(s):  
K Titani ◽  
T Shinoda ◽  
F W Putnam
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bence Jones Protein

Chemical structure of light chains: amino acid sequence of type K Bence-Jones proteins

1966 ◽  
Vol 166 (1003) ◽  
pp. 124-137 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Single Point ◽  
Structural Difference ◽  
Light Chains ◽  
Single Point Mutation ◽  
Amino Terminal ◽  
Type K ◽  
Bence Jones Proteins

Bence-Jones proteins are the light chains of the autologous myeloma globulin and are analogous to the light chains of normal human immunoglobulins. Peptide mapping has demonstrated that Bence-Jones proteins share a fixed portion of their sequence (the ‘constant’ portion) and also have a mutable part (the ‘variable’ portion). Sequence analysis and ordering of the tryptic and chymotryptic peptides has provided the tentative complete amino acid sequence of one Bence-Jones protein of antigenic type K. Comparison with partial sequence data for other type K Bence-Jones proteins has revealed many structural differences in the amino terminal half of the molecules, but only one structural difference in the carboxyl terminal half. The latter is strongly correlated with the Inv genetic factor. The points of interchange in the amino terminal half occur in clusters close to the half cystine residues and the ‘switch peptide’ (positions 102 through 105), after which the sequence becomes essentially invariant. This suggests that the major areas subject to sequence variation are part of a single topographical region which may define a portion of the antigen combining site in the light chains of antibodies. Many, but not all, the amino acid interchanges are compatible with a single point mutation. As yet, no single mutational theory suffices to explain the manifold differences in structure of the light chains. Such structural variation, however, could result from the presence of many related genes.

scholarly journals Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase

1971 ◽  
Vol 122 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley
Keyword(s):  
Amino Acid ◽  
Cyanogen Bromide ◽  
Triose Phosphate Isomerase ◽  
Amino Acid Sequences ◽  
Cysteine Residues ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Triose Phosphate ◽  
Methionine Residues ◽  
Polypeptide Chains

1. The nature of the subunits in rabbit muscle triose phosphate isomerase has been investigated. 2. Amino acid analyses show that there are five cysteine residues and two methionine residues/subunit. 3. The amino acid sequences around the cysteine residues have been determined; these account for about 75 residues. 4. Cleavage at the methionine residues with cyanogen bromide gave three fragments. 5. These results show that the subunits correspond to polypeptide chains, containing about 230 amino acid residues. The chains in triose phosphate isomerase seem to be shorter than those of other glycolytic enzymes.

scholarly journals Amino acid sequence around the reactive cysteine residues in thiolase

FEBS Letters ◽  
1968 ◽  
Vol 1 (3) ◽  
pp. 150-152 ◽  
Author(s):  
U. Gehring ◽  
J.Ieuan Harris
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cysteine Residues
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