Characterization of tryptic peptides from porcine haptoglobin light chain and an amino acid sequence

1976 ◽  
Vol 54 (1) ◽  
pp. 93-98 ◽  
Author(s):  
W. P. Chung ◽  
David B. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Electrophoretic Mobility ◽  
Light Chain ◽  
Light Chains ◽  
Tryptic Peptides ◽  
Partial Sequencing

The tryptic peptides derived from porcine haptoglobin light chains have been separated and characterized by composition, chromatography, electrophoretic mobility, and partial sequencing. Depending on homology with the corresponding human polypeptide, the amino acid sequence of the chain is proposed. Twenty differences from the human chain are indicated in the total of 84 residues.

scholarly journals A genetic polymorphism in the constant region of rabbit b4 kappa chains.

1976 ◽  
Vol 143 (6) ◽  
pp. 1475-1482 ◽  
Author(s):  
J A Sogn ◽  
T J Kindt
Keyword(s):  
Amino Acid ◽  
Genetic Polymorphism ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Light Chains ◽  
Amino Acid Substitutions ◽  
Constant Region ◽  
Inheritance Pattern ◽  
Amino Acid Sequence Analysis

Amino acid sequence analysis of a b4 light chain from a rabbit homogeneous antistreptococcal antibody revealed the presence of two amino acid substitutions in the constant region not previously reported for these positions. These interchanges, consisting of serine for alanine at position 121 and leucine for glutamine at position 124, were also present in about 30% of the pooled b4 light chains isolated from pooled IgG from the rabbit (4539) that produced the homogeneous antibody. In addition, these interchanges (b4var) were found, always at the same levels, in varying percentages in nonimmune or early immune bleedings from related rabbits in this pedigreed family and could be traced for five generations. The inheritance pattern of b4var was consistent with autosomal codominant inheritance.

scholarly journals Amino acid sequence of the N-terminal 139 residues of light chain derived from a homogeneous rabbit antibody

1974 ◽  
Vol 141 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Jean-Claude Jaton
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Peptide Bond ◽  
Complete Sequence ◽  
Light Chains ◽  
Rabbit Antibody ◽  
Arginine Residues ◽  
V Region ◽  
Combination Of Methods

The amino acid sequence of the N-terminal 139 residues of the L (light) chain derived from a homogeneous rabbit antibody (designated BS-1) to type III pneumococci was determined. A combination of methods involving tryptic cleavage restricted to the 2 arginine residues of the molecule and mild acid hydrolysis of a labile peptide bond between the V (variable) and C (constant) regions of the L chain (Fraser et al., 1972) allowed the isolation of two large peptides comprising the entire V region (residues 1–109); these peptides were suitable for automated Edman degradation. The complete sequence analysis of the V region was carried out with only 4μmol of L chain. This material was homogeneous, although minor variant sequences, if present at the 10% value, would not have been detected. The L chain contains 3 intrachain disulphide bridges, whose pairing was established by diagonal electrophoresis: there is one V-region bridge between positions 23 and 88 and one C-region bridge between positions 134 and 194; the third one connects V and C domains between positions 80 and 171. When compared with the basic sequence of human κ chains, rabbit L chain BS-1 appears to be more similar to the VKI prototype sequence than to VKII or VKIII sequences, where VKI, VKII and VKIII represent subgroups I, II and III respectively of V regions of κ light chains. The V regions of rabbit heavy and light chains are homologous to each other. The presence of two clusters of 3 glycine residues in positions 94–96 and 99–101 respectively is remarkable. Residues 94–96 may be related to antibody complementarity whereas residues 99–101 function probably as a pivot permitting the combining region of the L chain to make optimal contact with the antigenic determinant (Wu & Kabat, 1970).

scholarly journals Preparation of the alkali and P light chains of chicken gizzard myosin. Amino acid sequence of the alkali light chain

1983 ◽  
Vol 211 (1) ◽  
pp. 267-272 ◽  
Author(s):  
R J A Grand ◽  
S V Perry
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Binding Sites ◽  
Light Chains ◽  
British Library ◽  
Simple Method ◽  
Chicken Gizzard ◽  
High Affinity

1. A simple method is described for the purification of the alkali and P light chains from chicken gizzard myosin. 2. The sequence of the alkali light chain has been unequivocally determined, except for the N-terminal dipeptide, by using the tryptic and CNBr peptides. 3. No evidence was obtained for any specific high-affinity Ca2+-binding sites on the alkali light chain. 4. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50120 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1983) 209, 5.

scholarly journals A conserved human germline V kappa gene directly encodes rheumatoid factor light chains.

1986 ◽  
Vol 164 (6) ◽  
pp. 2119-2124 ◽  
Author(s):  
V Radoux ◽  
P P Chen ◽  
J A Sorge ◽  
D A Carson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Light Chains ◽  
Gene Repertoire ◽  
Rheumatoid Factors ◽  
Variable Regions ◽  
Normal People ◽  
Related Group ◽  
Full Length Gene

The full-length gene that encodes the light chain variable regions of an idiotypically related group of human IgM kappa rheumatoid factors (RFs) has been cloned and sequenced. The deduced amino acid sequence is identical to four separate RF proteins. These results prove that genes capable of encoding human anti-IgG autoantibody light chains without any somatic mutation are present in the kappa gene repertoire of normal people.

scholarly journals Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains.

1984 ◽  
Vol 4 (5) ◽  
pp. 956-965 ◽  
Author(s):  
S Falkenthal ◽  
V P Parker ◽  
W W Mattox ◽  
N Davidson
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Sequence Homology ◽  
Electrophoretic Pattern ◽  
In Vitro Translation ◽  
Light Chains ◽  
Chain Gene ◽  
Light Chain Gene

A chimeric lambda DNA molecule containing the myosin alkali light-chain gene of Drosophila melanogaster was isolated. The encoded amino acid sequence was determined from the nucleic acid sequence of a cDNA homologous to the genomic clone. The identity of the encoded protein was established by two criteria: (i) sequence homology with the chicken alkali light-chain proteins and (ii) comparison of the two-dimensional gel electrophoretic pattern of the peptides synthesized by in vitro translation of hybrid-selected RNA to that of myosin alkali light-chain peptides extracted from Drosophila myofibrils. There is only one myosin alkali light-chain in D. melanogaster; its chromosomal location is region 98B . This gene is abundantly expressed during the development of larval as well as adult muscles. The Drosophila protein appears to contain one putative divalent cation-binding domain (an EF hand) as compared with the three EF hands present in chicken alkali light chains.

scholarly journals Comparison of the amino acid sequences of the variable regions of light chains derived from two homogeneous rabbit anti-pneumococcal antibodies

1974 ◽  
Vol 141 (1) ◽  
pp. 15-25 ◽  
Author(s):  
Jean-Claude Jaton
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Amino Acid Sequences ◽  
Basic Sequence ◽  
Light Chains ◽  
Amino Acid Residues ◽  
Rabbit Antibody ◽  
Variable Regions ◽  
Type Iii

The amino acid sequence of the N-terminal 139 residues of the L (light) chain derived from a homogeneous rabbit antibody to type III pneumococci was determined. This L chain, designated BS-5, exhibits a greater degree of homology with the basic sequence of human κ chains of subgroup I (72%) than with subgroups II and III. L-chain BS-5 differs from another L chain (BS-1), also derived from an antibody to type III pneumococci (Jaton, 1974), by eight amino acid residues, even though the chains are identical within the N-terminal 30 residues. Six of these eight substitutions are located within the three hypervariable sections of the variable half: Asn/Ser in position 31, Glu/Ala in position 55, Asx/Thr, Thr/Gly, Thr/Gly and Val/Tyr in positions 92, 94, 96 and 97 respectively. The two anti-pneumococcal L chains BS-1 and BS-5 are much more similar to each other than to an anti-azobenzoate L chain (Appella et al., 1973), from which they differ by 30 and 29 residues respectively. Of these interchanges 13–15 are confined to the three hypervariable sections, and 11 occur within the N-terminal 27 positions. The three chains have an identical sequence from residue 98 to residue 139, except for a possible inversion of two residues in positions 130–131 of the anti-azobenzoate chain.

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains

1984 ◽  
Vol 4 (5) ◽  
pp. 956-965
Author(s):  
S Falkenthal ◽  
V P Parker ◽  
W W Mattox ◽  
N Davidson
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Sequence Homology ◽  
Electrophoretic Pattern ◽  
In Vitro Translation ◽  
Light Chains ◽  
Chain Gene ◽  
Light Chain Gene

A chimeric lambda DNA molecule containing the myosin alkali light-chain gene of Drosophila melanogaster was isolated. The encoded amino acid sequence was determined from the nucleic acid sequence of a cDNA homologous to the genomic clone. The identity of the encoded protein was established by two criteria: (i) sequence homology with the chicken alkali light-chain proteins and (ii) comparison of the two-dimensional gel electrophoretic pattern of the peptides synthesized by in vitro translation of hybrid-selected RNA to that of myosin alkali light-chain peptides extracted from Drosophila myofibrils. There is only one myosin alkali light-chain in D. melanogaster; its chromosomal location is region 98B . This gene is abundantly expressed during the development of larval as well as adult muscles. The Drosophila protein appears to contain one putative divalent cation-binding domain (an EF hand) as compared with the three EF hands present in chicken alkali light chains.

Antigenische Klassifizierung der Paraproteine und normalen Immunoglobuline vom Lambda-Typ / Paraproteins and Normal Immunoglobulins of the Lambda Type: Immunochemical Differentiation and Classification

1971 ◽  
Vol 26 (12) ◽  
pp. 1292-1302 ◽  
Author(s):  
F. W. Tischendorf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Basic Amino Acid ◽  
Light Chains ◽  
Antigenic Sites ◽  
Normal Individuals ◽  
Normal Light ◽  
Bence Jones Proteins

The elaboration of antisera recognizing antigenic sites of the variable region of pathological immunoglobulin λ chains (Bence-Jones-proteins) is described. The antisera react with the (St+) marker carried by Bence-Jones-proteins of the basic amino-acid sequence VλI and the (111+) marker carried by L-chains of the basic sequence VλIII. With these antisera three specificityregion subtypes of human λ immunoglobulin chains could be distinguished antigenically. Twenty randomly chosen normal individuals were shown to be associated with λ chains of both basic sequences, VλI and VλIII. The results provide evidence for the non-allelic nature of the two aminoterminal light chain forms (p<0.001) and suggest that the basic sequences VλI and VλIII of Bence-Jones-proteins represent two distinct subgroups of normal light chains.

Sign in / Sign up

Export Citation Format

Share Document