scholarly journals A blocked N-terminal residue in the light chain of rabbit immunoglobulin G

1968 ◽  
Vol 107 (4) ◽  
pp. 449-453 ◽  
Author(s):  
E. Rüde ◽  
D. Givol
Keyword(s):  
Carboxylic Acid ◽  
Light Chain ◽  
Immunoglobulin G ◽  
Terminal Sequence ◽  
Terminal Residue ◽  
Rabbit Immunoglobulin

The light chain of rabbit immunoglobulin G was shown to contain 15–20% blocked N-terminal residue. The blocked residue is pyrrolid-2-one-5-carboxylic acid, and most of the chains that contain this residue have the N-terminal sequence pyrrolid-2-one-5-carbonyl-valine.

scholarly journals Goat immunoglobin G. Peptide chains and terminal residues

1969 ◽  
Vol 115 (3) ◽  
pp. 371-375 ◽  
Author(s):  
D. Givol ◽  
E. Hurwitz
Keyword(s):  
Carboxylic Acid ◽  
Heavy Chain ◽  
Light Chain ◽  
Immunoglobulin G ◽  
Light Chains ◽  
Terminal Sequence ◽  
Terminal Residue ◽  
Heavy Chains ◽  
Molecular Weights ◽  
Immunoglobin G

Goat immunoglobulin G (IgG) was isolated and characterized. The molecular weights of the IgG and its heavy chains and light chains were found to be 144000, 53600 and 23000 respectively. The light chain corresponds to human L type as was shown by the absence of C-terminal S-carboxymethylcysteine and its high content of N-terminal pyrrolid-2-one-5-carboxylic acid (PCA). The major C-terminal residue of the light chain was serine and the major N-terminal dipeptide was PCA-Ala (0·6mole/mole). The major C-terminal residue of the heavy chain was glycine and the N-terminal sequence of the heavy chain is PCA-Val-Gln. This tripeptide was obtained in a 70% yield.

scholarly journals Variation in the N-terminal sequence of heavy chains of immunoglobulin G from rabbits of different allotype

1969 ◽  
Vol 112 (2) ◽  
pp. 173-185 ◽  
Author(s):  
J. M. Wilkinson
Keyword(s):  
Amino Acids ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Cyanogen Bromide ◽  
Terminal Sequence ◽  
Heavy Chains ◽  
Terminal Fragment ◽  
Rabbit Immunoglobulin

The sequences of the N-terminal peptides prepared by Pronase digestion of the heavy chain of rabbit immunoglobulin G of allotype Aa1, Aa2 and Aa3 were determined and were shown to be related to the allotype. An N-terminal fragment of about 34 residues was also prepared from the allotype heavy chains, by cleavage with cyanogen bromide; the yield varied with the allotype. The sequences of the cyanogen bromide fragments from the Aa1 and Aa3 heavy chains contain allotype-related variations similar to those found in the N-terminal Pronase peptides, and these sequences are thought to be representative of the whole heavy-chain populations. There is about 60% homology between the two sequences, and superimposed on the differences between them there are a number of positions within each sequence at which at least two amino acids are present.

LIPOPOLYSACCHARIDE-SENSITIVE SERINE-PROTEASE ZYMOGEN (FACTOR C) OF LIMULUS HEMOCYTES: IDENTIFICATION AND ALIGNMENT OF PROTEOLYTIC FRAGMENTS PRODUCED DURING THE ACTIVATION SHOW THAT IT IS A NOVEL TYPE OF SERINE-PROTEASE

1987 ◽  
Author(s):  
F Tokunaga ◽  
T Miyata ◽  
T Nakamura ◽  
T Morita ◽  
S Iwanaga
Keyword(s):  
Serine Protease ◽  
Heavy Chain ◽  
Light Chain ◽  
Interleukin 2 ◽  
Coagulation Factor ◽  
Clotting Factor ◽  
Single Chain ◽  
Terminal Sequence ◽  
A Chain ◽  
Factor C

Limulus clotting factor, factor C, is a lipopolysaccharide (LPS)-sensitive serine-protease zymogen present in the hemocytes. It is a two-chain glycoprotein (M.W. = 123,000) composed of a heavy chain (M.W. = 80,000) and a light chain (M.W. = 43,000) T. Nakamura et al. (1986) Eur. J. Biochem. 154, 511-521 .On further studies of this zymogen, a single-chain factor C (M.W. = 123,000) was identified by Western blotting technique. The heavy chain had an NH2-terminal sequence of Ser-Gly-Val-Asp-, which was consistent with the NH2-terminal sequence of the single-chain factor C, indicating that the heavy chain is located in the NH2-terminal part of the zymogen. The light chain had an NH22-terminal sequence of Ser-Ser-Gln-Pro-. Incubation of the two-chain zymogen with LPS resulted in the cleavage of a Phe-Ile bond between residues 72 and 73 of the light chain. Concomitant with this cleavage, the A (72.amino acids) and B chains derived from the light chain was formed. The complete amino acid sequence of the A chain was determined by automated Edman degradation. The A chain contained a typical segment which is similar structuraly to those a family of repeats in human β2 -glycoprotein I, complement factors B, Clr, Cls, H, C4b-binding protein, 02, coagulation factor XIII b subunit, haptoglobin a chain, and interleukin 2 receptor. The NH2-terminal sequence of the B chain was Ile-Trp-Asn-Gly-. This chain contained the serine-active site sequence of -ASP-Ala-Cys-Ser-Gly-Asp-SER-Gly-Gly-Pro-.These results indicate that limulus factor C exists in the hemocytes in a single-chain zymogen form and is converted to an active serine-protease by hydrolysis of a specific Phe-Ile peptide bond. The correlation of limulus factor C and mammalian complement proteins was also suggested.

scholarly journals Limited proteolysis of complement components C2 and factor B. Structural analogy and limited sequence homology

1979 ◽  
Vol 183 (3) ◽  
pp. 615-622 ◽  
Author(s):  
M A Kerr
Keyword(s):  
Sequence Homology ◽  
Polyacrylamide Gel Electrophoresis ◽  
Limited Proteolysis ◽  
Gel Filtration ◽  
Serine Proteinase ◽  
Terminal Sequence ◽  
Complement Components ◽  
Factor B ◽  
Terminal Residue ◽  
Covalently Linked

A method is described for the simultaneous purification of milligram quantities of complement components C2 and Factor B. Both products are homogeneous by the criteria of polyacrylamide-gel electrophoresis and N-terminal sequence analysis. Component C2 is cleaved by serine proteinase C1s at an X-Lys bond to give fragment C2a (approx. mol.wt. 74000) and fragment C2b (approx. mol.wt. 34000). The two fragments can be separated by gel filtration without the need for reducing or denaturing agents. Fragment C2b represents the N-terminal end of the molecule. Similar results were seen on cleavage of Factor B by Factor D in the presence of component C3. Again two non-covalently linked fragments are formed. The smaller, fragment Ba (approx. mol.wt. 36,000),) has threonine as the N-terminal residue, as does Factor B; the larger, fragment Bb (approx. mol. wt. 58000), has lysine as the N-terminal residue. A similar cleavage pattern is obtained on limited proteolysis of Factor B by trypsin, suggesting an Arg-Lys-or Lys-Lys bond at the point of cleavage. Although component C2 and Factor B show no apparent N-terminal sequence homology, a limited degree of sequence homology is seen around the sites of proteolytic cleavage.

scholarly journals Karyotype of a mouse/rabbit hybrid clone secreting rabbit immunoglobulin x light chain

Hereditas ◽  
2008 ◽  
Vol 98 (1) ◽  
pp. 83-87 ◽  
Author(s):  
H. A. SUOMALAINEN ◽  
L. BRYS ◽  
W. VAN DER LOO ◽  
J. SCHRÖDER
Keyword(s):  
Light Chain ◽  
Hybrid Clone ◽  
Rabbit Immunoglobulin

scholarly journals A second rabbit kappa isotype.

1982 ◽  
Vol 156 (2) ◽  
pp. 585-595 ◽  
Author(s):  
A Benammar ◽  
P A Cazenave
Keyword(s):  
Light Chain ◽  
Immunoglobulin G ◽  
Antigenic Determinants ◽  
Gene Encoding ◽  
Genetic Studies ◽  
B Locus ◽  
Different Populations ◽  
Domestic Rabbits ◽  
Chain Type

Immunoglobulin G (IgG) from the rabbit strain Basilea was previously shown to contain two distinct populations of molecules one with light chain belonging to the known lambda isotype and the others to a new kappa-like L chain type. Alloantisera prepared against the Basilea IgG are directed against the kappa-like light chain (anti-bas antisera). All Basilea rabbits express kappa-like chains recognized by anti-bas sera, but IgG from other domestic rabbits did not react with these antisera. Genetic studies of wild rabbits belonging to different populations show that the bas+ phenotype could be found in heterozygous rabbits as well as those homozygous at the b locus. The gene encoding the bas+ light chain is closely linked to the b locus. Moreover, antigenic determinants recognized by anti-bas antibodies and antigenic determinants recognized by antibodies directed against allotypic determinants of the b series are located on distinct IgG molecules. These results show that there are two rabbit kappa isotypes: the kappa 1 isotype, bearing allotypic determinants of the b series, and the kappa 2 isotype, for which bas+ chain is one of the allotypic forms. The kappa 1 and kappa 2 isotypes are controlled by closely linked genes.

scholarly journals The N-terminal sequence of the heavy chain of rabbit immunoglobulin IgG

1966 ◽  
Vol 100 (2) ◽  
pp. 303-308 ◽  
Author(s):  
JM Wilkinson ◽  
EM Press ◽  
RR Porter
Keyword(s):  
Heavy Chain ◽  
Terminal Sequence ◽  
Rabbit Immunoglobulin
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