scholarly journals The amino acid sequence of rabbit J chain in secretory immunoglobulin A

1990 ◽  
Vol 271 (3) ◽  
pp. 641-647 ◽  
Author(s):  
G J Hughes ◽  
S Frutiger ◽  
N Paquet ◽  
J C Jaton
Keyword(s):  
Amino Acid ◽  
Immunoglobulin A ◽  
Complete Sequence ◽  
Glycosylation Site ◽  
Secretory Iga ◽  
Amino Acid Residues ◽  
J Chain ◽  
Mouse Sequence ◽  
Human Sequence ◽  
One Step

The primary structure of rabbit J chain, which occurs covalently bound to secretory IgA, was determined. J chain was isolated in its S-carboxymethylated form, in one step, by SDS/PAGE followed by electro-elution; 5 nmol of protein (approx. 75 micrograms), in all, was necessary for the determination of the complete sequence by the ‘shot-gun’ microsquencing technique; with the use of several site-specific endoproteinases, the various digests of S-carboxymethylated J chain were separated by micro-bore reverse-phase h.p.l.c. and the partial N-terminal sequences of all peptides were analysed. From the sequence alignment, gaps were filled by further extensive sequencing of the relevant overlapping fragments isolated from selected digests. Rabbit J chain comprises 136 amino acid residues, out of which eight are conserved cysteine residues, and is more closely similar to the human sequence (73.5% identify) than to the mouse sequence (68% identity). There is one unique glycosylation site at asparagine-48.

Structure of immunoglobulin A. Amino acid sequence of cysteine-containing peptides from the J chain

Biochemistry ◽  
1973 ◽  
Vol 12 (6) ◽  
pp. 1119-1124 ◽  
Author(s):  
E. Mendez ◽  
B. Frangione ◽  
E. C. Franklin
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Immunoglobulin A ◽  
J Chain

scholarly journals Complementary DNA sequence of human amyloidogenic immunoglobulin light-chain precursors

1992 ◽  
Vol 285 (1) ◽  
pp. 149-152 ◽  
Author(s):  
P Aucouturier ◽  
A A Khamlichi ◽  
J L Preud'homme ◽  
M Bauwens ◽  
G Touchard ◽  
...  
Keyword(s):  
Amino Acid ◽  
Light Chain ◽  
Bone Marrow Cells ◽  
Northern Blotting ◽  
Glycosylation Site ◽  
Light Chains ◽  
Amino Acid Residues ◽  
Complementary Dna ◽  
Kidney Glomerulus ◽  
Complementarity Determining Regions

The primary structure of three amyloid precursor light chains was deduced from the sequence of complementary DNA (cDNA) from bone marrow cells from patients affected with classical lambda (patient Air) or kappa (patient Arn) amyloidosis and from a patient (Aub) in whom lambda amyloid deposits were unusual by their perimembranous location in the kidney glomerulus. All three RNAs were of normal size, as estimated by Northern blotting, and encoded normal-sized light chains. The deduced light-chain sequence from patient Arn was related to the V kappa 1 subgroup, and included ten residues that had not been previously reported at these positions, only one of which (Leu-21) was located in a beta-sheet (4-2). The unusual presence of Asn-70 determined a potential N-glycosylation site. The sequence of the light chain from patient Air belonged to the V lambda 1 subgroup, and included three unusually located amino acid residues, one of which had already been reported in an amyloidogenic lambda-chain. The sequence of the light chain from patient Aub was related to the V lambda 3 subgroup, and contained five amino acid residues that had not previously been described at the corresponding positions; two of them (His-36 and Ser-77) were located in beta-sheets (3-1 and 4-3 respectively). This sequence was also peculiar because of the presence of numerous acidic residues in the complementarity-determining regions. Such unusual primary structures might be responsible for the amyloidogenic properties of these light-chain precursors.

scholarly journals Molecular-scale features that govern the effects of O-glycosylation on a carbohydrate-binding module

2015 ◽  
Vol 6 (12) ◽  
pp. 7185-7189 ◽  
Author(s):  
Xiaoyang Guan ◽  
Patrick K. Chaffey ◽  
Chen Zeng ◽  
Eric R. Greene ◽  
Liqun Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glycosylation Site ◽  
Glycan Structure ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Amino Acid Residues ◽  
Glycosidic Linkage ◽  
Molecular Scale

The importance of the glycan structure and size, amino acid residues near the glycosylation site, and glycosidic linkage in controlling the effects of CBMO-glycosylation is shown.

scholarly journals On the Primary Structure of Human Fibrinogen

1977 ◽  
Author(s):  
A. Henschen ◽  
F. Lottspeich ◽  
E. Töpfer-Petersen ◽  
R. Warbinek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Cyanogen Bromide ◽  
Attachment Site ◽  
Complete Sequence ◽  
Cleavage Sites ◽  
Amino Acid Residues ◽  
Human Fibrinogen ◽  
Β Chain

The aim of the present investigation is to elucidate the primary structure of human fibrinogen. Through the work of several laboratories including our own large parts of the structure are now known. Here will be reported the complete amino acid sequence of the γ-chain (409 residues). Furthermore, the carbohydrate linkage site in the β-chain and plasmin cleavage sites in the β- and γ-chains have been identified.The peptide chains were isolated by CM-cellulose chromatography following mercaptolysis and alkylation. The γ-chain was cleaved in a way to produce large fragments suitable for automatic sequencing, e. g. with cyanogen bromide or trypsin after citraconylation. The sequences of the isolated fragments allowed reconstruction of the complete sequence of the γ-chain.The carbohydrate linkage site in the β-chain could be isolated by affinity chromatography on concanavalin A-agarose following cleavage of the chain by trypsin or cyanogen bromide. The sequence of 21 amino acid residues around the carbohydrate attachment site was determined.The plasmin cleavage site giving rise to N-terminal glycine in the γ-chain D-fragment was identified. The amino acid sequence linking plasmic fragments E and D in the β-chain was determined.

scholarly journals Primary structure of a structural protein from the cuticle of the migratory locust, Locusta migratoria

1986 ◽  
Vol 236 (3) ◽  
pp. 713-720 ◽  
Author(s):  
P Højrup ◽  
S O Andersen ◽  
P Roepstorff
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Locusta Migratoria ◽  
Protein A ◽  
Complete Sequence ◽  
Amino Acid Residues ◽  
Structural Protein ◽  
Migratory Locust ◽  
Common Amino Acid ◽  
Conserved Sequence

The complete amino acid sequence of a structural protein isolated from pharate cuticle of the locust Locusta migratoria was determined. The protein has an unusual amino acid composition: 42% of the residues are alanine and only 14 of the 20 common amino acid residues are present. The primary structure consists of regions enriched in particular amino acid residues. The N-terminal region and a region close to the C-terminus are enriched in glycine. The rest of the protein is dominated by alanine, except for two short regions enriched in hydrophilic residues. Almost all the proline residues are situated in the alanine-rich regions in a conserved sequence ‘A-A-P-A/V’. An internal duplication has taken place covering most of the protein except for the glycine-rich regions. Owing to the unusual features of the protein a combination of automated Edman degradations and plasma-desorption m.s. was used to determine the complete sequence. The protein does not show sequence homology to other proteins, but proteins divided into regions enriched in the same kind of amino acid residues have been isolated from other insect structures.

scholarly journals Comparison of the amino acid sequences of the variable domains of two homogeneous rabbit antibodies to type III pneumococcal polysaccharide

1975 ◽  
Vol 147 (2) ◽  
pp. 235-247 ◽  
Author(s):  
J C Jaton
Keyword(s):  
Amino Acid ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Amino Acid Residues ◽  
Rabbit Antibody ◽  
Variable Regions ◽  
Type Iii ◽  
Variable Domains ◽  
V Region

The amino acid sequences of the V (variable) regions of the H (heavy) and L (light) chains derived from rabbit antibody K-25, specific for type III pneumococci, were determined; this is the second homogeneous rabbit antibody besides antibody BS-5 whose complete sequence of the V domain has been established (Jaton, 1974d). The V regions of L chains BS-5 and K-25 (both of allotype b4) differ from each other by 19 amino acid residues; 11 of these 19 substitutions are located within the three hypervariable sections of the V region. On the basis of seven amino acid differences within the N-terminal 28 positions, it is suggested that L chain K-25 belongs to a different subgroup of rabbit K chains and L chain BS-5. H chain K-25 (allotype a2) differs from another H chain of the same allotype by one amino acid substitution within the N-terminal 70 positions in addition to interchanges occurring in the first two hypervariable sections. H chain K-25 was compared with H chain BS-5 (allotype a1) and with the known V-region rabbit sequences. Allotype-related differences between a1, a2 and a3 chains appear to occur within the N-terminal 16 positions and possibly in scattered positions throughout the V-region. In the hypervariable positions, variability between the two antibodies is remarkably more pronounced within the third hypervariable section of both H and L chains than within the first two.

scholarly journals Complete sequence of the human mucin MUC4: a putative cell membrane-associated mucin

1999 ◽  
Vol 338 (2) ◽  
pp. 325-333 ◽  
Author(s):  
Nicolas MONIAUX ◽  
Séverine NOLLET ◽  
Nicole PORCHET ◽  
Pierre DEGAND ◽  
Anne LAINE ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Signalling ◽  
Complete Sequence ◽  
Surface Glycoprotein ◽  
Amino Acid Residues ◽  
Cell Surface Glycoprotein ◽  
Differentiated Cells ◽  
C Terminus ◽  
Sialomucin Complex ◽  
Central Sequences

The MUC4 gene, which encodes a human epithelial mucin, is expressed in various epithelial tissues, just as well in adult as in poorly differentiated cells in the embryo and fetus. Its N-terminus and central sequences have previously been reported as comprising a 27-residue peptide signal, followed by a large domain varying in length from 3285 to 7285 amino acid residues. The present study establishes the whole coding sequence of MUC4 in which the C-terminus is 1156 amino acid residues long and shares a high degree of similarity with the rat sialomucin complex (SMC). SMC is a heterodimeric glycoprotein complex composed of mucin (ascites sialoglycoprotein 1, ASGP-1) and transmembrane (ASGP-2) subunits. The same organization is found in MUC4, where the presence of a GlyAspProHis proteolytic site may cleave the large precursor into two subunits, MUC4α and MUC4β. Like ASGP-2, which binds the receptor tyrosine kinase p185neu, MUC4β possesses two epidermal growth factor-like domains, a transmembrane sequence and a potential phosphorylated site. MUC4, the human homologue of rat SMC, may be a heterodimeric bifunctional cell-surface glycoprotein of 2.12 µm. These results confer a new biological role for MUC4 as a ligand for ErbB2 in cell signalling.

Cloning, expression, and tissue localization of the calcium-sensing receptor in chicken (Gallus domesticus)

1997 ◽  
Vol 273 (3) ◽  
pp. R1008-R1016 ◽  
Author(s):  
R. Diaz ◽  
S. Hurwitz ◽  
N. Chattopadhyay ◽  
M. Pines ◽  
Y. Yang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Messenger Rna ◽  
Hormone Secretion ◽  
Amino Acid Identity ◽  
Gallus Domesticus ◽  
Northern Analysis ◽  
Xenopus Laevis Oocytes ◽  
Amino Acid Residues ◽  
Human Sequence ◽  
Intracellular Ca

In previous studies, we characterized an extracellular Ca2+ (Cao(2+))-sensing receptor (CaR) that plays a central role in regulating parathyroid hormone secretion in mammals by sensing Cao2+. In the present study, we have cloned and characterized the chicken (Gallus domesticus) homolog of the CaR. The chicken parathyroid CaR shares a high degree of homology (84% amino acid identity) with the human CaR and displays a similar topology. Moreover, amino acid residues where mutations cause disorders of Cao(2+)-sensing in the human CaR share the wild-type human sequence in the chicken CaR. However, a single region in the extracellular domain of the chicken CaR differs substantially from its mammalian homologs. Xenopus laevis oocytes injected with chicken CaR cRNA respond to elevated ambient levels of Cao2+, extracellular Mg2+, or extracellular Gd3+ with the characteristic activation of inositol trisphosphate-dependent, intracellular Ca(2+)-induced Cl- currents elicited by mammalian CaRs as well as by G protein-linked receptors coupled to activation of phospholipase C. By in situ hybridization, clusters of cells in chicken parathyroid glands were shown to express CaR messenger RNA. Northern analysis and immunohistochemistry demonstrated expression of receptor transcripts and/or protein in kidney tubules and intestine as well as in brain. The close conservation of the amino acid sequence of the chicken CaR with its mammalian homologs as well as its similar tissue distribution suggest that the receptor may also play an important role in avian calcium homeostasis.

scholarly journals Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme

2000 ◽  
Vol 348 (3) ◽  
pp. 507-515 ◽  
Author(s):  
Ralph MELCHER ◽  
Alexandra HILLEBRAND ◽  
Ute BAHR ◽  
Bernd SCHRÖDER ◽  
Michael KARAS ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glycosylation Site ◽  
The Other ◽  
Selective Synthesis ◽  
Amino Acid Residues ◽  
Human Lysozyme ◽  
Glycosylation Sites ◽  
Site Selective

We have studied the elongation of oligosaccharides containing N-acetyl-lactosamine repeats using glycosylated human lysozyme mutants as a model. We reported previously that a combination of glycosylation sites at the 49th (site IV) and 68th (site II) amino acid residues of the protein particularly stimulates the synthesis of N-acetyl-lactosamine repeats [Melcher, Grosch, Grosse and Hasilik (1998) Glycoconjugate J. 15, 987-993]. In the present study we show that it is the carbohydrate attached to site IV that is selectively affected. It contains more N-acetyl-lactosamine repeats when site II is glycosylated in the same molecule. As a corollary of the glycosylation at site II, the synthesis of a third antenna at site IV is increased. The triantennary oligosaccharides at site IV contain more N-acetyl-lactosamine repeats than the biantennary ones. Thus placing a carbohydrate at site II stimulates the branching and the elongation of the carbohydrate at the other site.

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