THE PRIMARY STRUCTURE OF α2‐MACROGLOBULIN AND LOCALIZATION OF A FACTOR XIIIa CROSS‐LINKING SITEa

Sottrup‐Jensen, Lars; Stepanik, T M; Wierzbicki, Diane M.; Jones, C M; Lønblad, P B; Kristensen, Torsten Nygaard; Mortensen, Shila; Petersen, Torben E.; Magnusson, Staffan

doi:10.1111/j.1749-6632.1983.tb18091.x

Cited by 80 publications

(37 citation statements)

References 39 publications

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“…After electroblotting onto a ProBlott membrane, each band was excised and its composition determined. The amino acid compositions were as expected for residues 1314--1451 of human e2M [27]. The two bands at 22 kDa were found to contain 5.0 mol GlcNH2/mol RBD, indicating full glycosylation of its single site [27], whereas the 15-kDa band contained none, indicating no glycosylation.…”

Section: Lsoforms Of Rbdsupporting

confidence: 65%

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

Dolmer¹,

Jenner²,

Jacobsen³

et al. 1995

FEBS Letters

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Section: Lsoforms Of Rbdsupporting

confidence: 65%

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

Dolmer¹,

Jenner²,

Jacobsen³

et al. 1995

FEBS Letters

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“…Although two residues were obtained in each cycle, both structures could be identified because of the difference in recovery between the two peptides. The structures deduced were homologous with two different regions in the known primary structure of the human form of the protein [18]. Thus, the minor peptide was tentatively identified as Ser-49-Lys-58, containing no radioactivity, and the major peptide as Asn-938-Arg-956, containing all the radioactivity.…”

Section: Resultsmentioning

confidence: 80%

“…Comparison of the structures around the thioester bond in the subunits of human (top) and bovine (bottom) cY2-macroglobulin. The bovine protein structure is from the present analysis (table l), the human one and the numbering system (above the top line) are from [18]. The two established amino acid exchanges are boxed, as well as the probable difference at position 937, where an Arg or Lys (indicated by R/K) in the bovine inhibitor is indirectly deduced from the major tryptic cleavage that has occurred after this site.…”

mentioning

confidence: 99%

The structure around the thioester bond in bovine α₂‐macroglobulin

Björk

Jörnvall

1986

FEBS Letters

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The residues contributing to the thioester bonds in bovine q-macroglobulin were differentially labelled by modification of the Glu moiety with [Y]methylamine and of the Cys moiety with iodo[3H]acetate. The labelled region was identified and analyzed in a tryptic peptide. Two amino acid replacements between human and bovine q-macroglobulin were found at positions + 3 (Val/Ala) and +4 (Leu/Arg) from the Glu moiety of the thioester. Thus, marked differences exist between the human and bovine proteins in side chain size and charge close to the thioester bonds. These differences may explain the greater conformational stability of bovine a:-macroglobulin, compared with that of the human inhibitor, after cleavage of the thioester bonds. r?-Macroglobulin Protease inhibitor Thioester

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“…This moderate difference in affinity may well be due to structural differences between the rat and human macroglobulins (cf. [17]). In any case, it seems appropriate, in view of the present results, to use human a2-macroglobulin complexes in studies employing the rat as the experimental animal.…”

Section: Resultsmentioning

confidence: 99%

Uptake of rat and human α₂‐macroglobulin‐trypsin complexes into rat and human cells

et al. 1985

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Uptake of rat and human cc,-macroglobulin-trypsin complexes was measured in rat hepatocytes, rat and human adipocytes and human fibroblasts. Uptake and degradation of 1251-labelled rat complex were about one-third of that of the human complex in the various isolated cell types. In rat hepatocytes, the apparent K,,, for cell association of the rat complex was about 16 nM as compared to about 6 nM for the human complex. The V,,, values were similar, about 1 x lo4 molecules cell-l min-1. Thus, rat cr,-macroglobulin (an acute-phase protein) complexed with trypsin follows the same pathways of uptake as the human homologue, although with a somewhat lower affinity for the uptake system.

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THE PRIMARY STRUCTURE OF α₂‐MACROGLOBULIN AND LOCALIZATION OF A FACTOR XIII_a CROSS‐LINKING SITE^a

Cited by 80 publications

References 39 publications

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

The structure around the thioester bond in bovine α₂‐macroglobulin

Uptake of rat and human α₂‐macroglobulin‐trypsin complexes into rat and human cells

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THE PRIMARY STRUCTURE OF α2‐MACROGLOBULIN AND LOCALIZATION OF A FACTOR XIIIa CROSS‐LINKING SITEa

Cited by 80 publications

References 39 publications

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α2‐macroglobulin

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α2‐macroglobulin

The structure around the thioester bond in bovine α2‐macroglobulin

Uptake of rat and human α2‐macroglobulin‐trypsin complexes into rat and human cells

Contact Info

Product

Resources

About

THE PRIMARY STRUCTURE OF α₂‐MACROGLOBULIN AND LOCALIZATION OF A FACTOR XIII_a CROSS‐LINKING SITE^a

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α₂‐macroglobulin

The structure around the thioester bond in bovine α₂‐macroglobulin

Uptake of rat and human α₂‐macroglobulin‐trypsin complexes into rat and human cells