EurekaMag.com logo
+ Translate

The primary structure of mu chain disease protein bot peculiar amino acid sequence of the amino terminal 42 positions


, : The primary structure of mu chain disease protein bot peculiar amino acid sequence of the amino terminal 42 positions. Hoppe-Seyler's Zeitschrift fuer Physiologische Chemie 365(1): 105-118

The complete primary structure of the .mu. H-chain disease (.mu.-HCD) protein BOT was determined [in humans]. The monomeric HCD-.mu.-chain consists of 391 amino-acid residues, lacking the VH [H chain, variable part] and .mu.CH1 [1st domain of IgM H chain, constant part] domains but including the entire CH2, CH3 and CH4 domains (349 residues). The sequence of the preceeding 42 N-terminal residues which is designated as the pre-C-part presents no homology to any known variable or constant Ig sequence, but contains an internal homology of positions 10-19 to positions 20-29. The origin of the pre-C-part structure and the deletion of the .mu.CH1 domain of protein BOT are discussed.

(PDF 0-2 workdays service)

Accession: 006740944

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Barnikol-Watanabe, S.; Mihaesco, E.; Mihaesco, C.; Barnikol, H.U.; Hilschmann, N., 1984: The primary structure of mu-chain-disease protein BOT. Peculiar amino-acid sequence of the N-terminal 42 positions. The complete primary structure of the mu heavy-chain disease (mu-HCD) protein BOT has been determined. The monomeric HCD-mu-chain consists of 391 amino-acid residues, lacking the VH and mu CH1 domains but including the entire CH2, CH3 and CH4 doma...

Kratzin, H.; Yang, C.Y.; Goetz, H.; Pauly, E.; Koebel, S.; Egert, G.; Thinnes, F.P.; Wernet, P.; Altevogt, P.; Hilschmann, N., 1981: Primary structure of class ii hla 1. amino acid sequence of the amino terminal 198 residues of the beta chain of a hla dw 2 2 dr 2 2 allo antigen. The .beta.-chains of HLA-D/DR antigens from a lymphoblastoid homozygous cell line (HLA-A3,3;B7,7;-DW2,2;DR2,2) were purified by an exclusively chemical 3-step procedure: Nonidet P-40/CM-cellulose ion-exchange; sodium-dodecyl sulfate[SDS]/sephacryl...

Yang, C.Y.; Kratzin, H.; Goetz, H.; Thinnes, F.P.; Kruse, T.; Egert, G.; Koelbel, E.P.S.; Wernet, P.; Hilschmann, N., 1982: Primary structure of class ii human histo compatibility antigens 2. amino acid sequence of the amino terminal 179 residues of the alpha chain of an hla dw 2 dr 2 allo antigen. From a lymphoblastoid homozygous cell line (HLA-A3,3;B7,7;Dw2,2;DR2,2) the .alpha.-chain of the HLA-Dw2/DR2 antigen was isolated by an exclusively chemical procedure. The .alpha.- was separated from the .beta.-chain by chromatography with hydroxyl...

D.C.ro A.M.; Adrich Z.; Fournet B.; Capon C.; Bonicel J.J.; D.C.ro J.D.; Rovery M., 1989: Amino terminal sequence extension in the glycosylated forms of human pancreatic stone protein the 5 oxoproline amino terminal chain is o glycosylated on the 5th amino acid residue. The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond. Among the eleven amino acids of the...

Uehara H.; Ewenstein B.M.; Martinko J.M.; Nathenson S.G.; Coligan J.E.; Kindt T.J., 1980: Primary structure of murine major histo compatibility complex allo antigens amino acid sequence of the amino terminal 173 residues of the h 2k b glyco protein. The amino-terminal 173 residues of the murine histocompatibility antigen H-2Kb were assigned by using radiochemical methodology. The complete sequence of an 86 residue glycopeptide (CN-Ib), which is 1 of the 5 major CNBr fragments of Kb, was deter...

Maloy W.L.; Nathenson S.G.; Coligan J.E., 1981: Primary structure of murine major histo compatibility complex allo antigens amino acid sequence of the amino terminal 98 residues of the h 2d b glyco protein. The NH2-terminal 98 amino acid residues of the murine histocompatibility antigen H-2Db were assigned using radiochemical methodology. This represents the 1st extensive, continuous sequence information for a histocompatibility antigen encoded by th...

Moonen P.; Akeroyd R.; Westerman J.; Puijk W.C.; Smits P.; Wirtz K.W.A., 1980: The primary structure of the phosphatidyl choline exchange protein from bovine liver isolation and characterization of the staphylococcal protease peptides and the amino acid sequence of the amino terminal half residues 1 122. The phosphatidylcholine exchange protein from bovine liver consists of a single polypeptide chain and has a blocked N terminus. The protein contains an estimated 244 amino acid residues in accordance with a determined MW of 28,000. The protease fr...

Van-Loon-Klaassen, L.A.H.; Cuypers, H.T.; Van-Westreenen, H.; De-Jong, W.W.; Bloemendal, H., 1980: The primary structure of bovine lens leucine amino peptidase ec 3.4.11.1 complete amino acid sequence of the amino terminal cyanogen bromide fragment and site of limited tryptic digestion. The amino acid sequence of the N-terminal cyanogen bromide fragment of bovine lens leucine aminopeptidase was determined. This fragment contains 171 amino acid residues and has a calculated MW of 18,637. The sequence data presented here represent...

Monastyrskaya G.S.; Gubanov V.V.; Gur'ev S.O.; Lipkin V.M.; Sverdlov E.D., 1980: Primary structure of rna polymerase from escherichia coli nucleotide sequence of the rpob gene fragment and corresponding amino terminal amino acid sequence of the beta subunit. During the investigation of primary structures of E. coli DNA-dependent RNA polymerase .beta.-subunit and its structural gene rpoB, the nucleotide sequence of part of the EcoRI G fragment (645 base pairs), coding for the .beta.-subunit N-terminus,...

Butler, W.T.; Miller, E.J.; Finch, J.E.J., 1976: The covalent structure of cartilage collagen amino acid sequence of the amino terminal helical portion of the alpha 1 chain. The amino acid sequence of 162 residues from the NH2-terminal region of bovine .alpha.1(II) is reported. Automated sequence analysis of chains from pepsin-treated type II collagen indicated the sequence and order of 2 CNBr peptides, .alpha.1(II)-C...