Fine specificity of idiotope suppression in the A/J anti-azophenylarsonate response.

Two hapten-inhibitable murine monoclonal antiidiotopic antibodies identified two idiotopes expressed by the heavy chain of hybridoma protein 36-65, whose amino acid sequence is encoded in the germ line of A/J mice. Among cross-reactive idiotype-positive hybridoma proteins and p-azophenylarsonate-immune antibodies, the two idiotopes were not always expressed together; some diversified antibodies expressed one idiotope without the other. Suppression that was induced by the two antiidiotopes was idiotope specific and corresponded to the fine specificities of these two reagents.

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Arrangement of the disulphide bridges in human low-Mr kininogen

Biochemical Journal ◽

10.1042/bj2470015 ◽

1987 ◽

Vol 247 (1) ◽

pp. 15-21 ◽

Cited By ~ 26

Author(s):

J Kellermann ◽

C Thelen ◽

F Lottspeich ◽

A Henschen ◽

R Vogel ◽

...

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Light Chain ◽

The Other ◽

Critical Importance

The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.

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C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19801144 ◽

1980 ◽

Vol 45 (4) ◽

pp. 1144-1154 ◽

Cited By ~ 3

Author(s):

Miroslav Baudyš ◽

Helena Keilová ◽

Vladimír Kostka

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

The Other ◽

Terminal Sequence ◽

Terminal Part ◽

Terminal Amino Acid ◽

Tryptic Peptides ◽

Terminal Amino ◽

High Degree ◽

Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

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Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor).

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89026-3 ◽

1985 ◽

Vol 260 (9) ◽

pp. 5328-5341 ◽

Cited By ~ 8

Author(s):

B A McMullen ◽

K Fujikawa

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Hageman Factor ◽

Factor Xiia ◽

Alpha Factor

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Amino acid sequence of a mouse myeloma immunoglobin heavy chain (MOPC 47 A) with a 100-residue deletion.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)86502-x ◽

1979 ◽

Vol 254 (22) ◽

pp. 11418-11430

Author(s):

E.A. Robinson ◽

E. Appella

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Mouse Myeloma

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Stereotyped patterns of somatic hypermutation in subsets of patients with chronic lymphocytic leukemia: implications for the role of antigen selection in leukemogenesis

Blood ◽

10.1182/blood-2007-07-099564 ◽

2008 ◽

Vol 111 (3) ◽

pp. 1524-1533 ◽

Cited By ~ 226

Author(s):

Fiona Murray ◽

Nikos Darzentas ◽

Anastasia Hadzidimitriou ◽

Gerard Tobin ◽

Myriam Boudjogra ◽

...

Keyword(s):

Amino Acid ◽

Chronic Lymphocytic Leukemia ◽

Heavy Chain ◽

Germ Line ◽

Somatic Hypermutation ◽

Lymphocytic Leukemia ◽

Chain Gene ◽

Distinctive Features ◽

Ighv Gene ◽

Gene Usage

Abstract Somatic hypermutation (SHM) features in a series of 1967 immunoglobulin heavy chain gene (IGH) rearrangements obtained from patients with chronic lymphocytic leukemia (CLL) were examined and compared with IGH sequences from non-CLL B cells available in public databases. SHM analysis was performed for all 1290 CLL sequences in this cohort with less than 100% identity to germ line. At the cohort level, SHM patterns were typical of a canonical SHM process. However, important differences emerged from the analysis of certain subgroups of CLL sequences defined by: (1) IGHV gene usage, (2) presence of stereotyped heavy chain complementarity-determining region 3 (HCDR3) sequences, and (3) mutational load. Recurrent, “stereotyped” amino acid changes occurred across the entire IGHV region in CLL subsets carrying stereotyped HCDR3 sequences, especially those expressing the IGHV3-21 and IGHV4-34 genes. These mutations are underrepresented among non-CLL sequences and thus can be considered as CLL-biased. Furthermore, it was shown that even a low level of mutations may be functionally relevant, given that stereotyped amino acid changes can be found in subsets of minimally mutated cases. The precise targeting and distinctive features of somatic hypermutation (SHM) in selected subgroups of CLL patients provide further evidence for selection by specific antigenic element(s).

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