Identification of the disulfide bonds of the human complement component C3

Schaller, Johann; Söhndel, Sabine; Rickli, Egon E.

doi:10.1007/bf01673745

Cited by 2 publications

(2 citation statements)

References 6 publications

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“…k Bis-PTH-Cys, was seen in cycle 2. description of the bridges in C3 [23] is consistent with the results described here. Together with previous cDNA analysis [9], localization of an internal thiol ester [4], determination of 3 bridges in C3a [14], structure determination of high-mannose-type carbohydrate groups [20,21] attached to Asn63 and Asn917 [22] the primary structure determination of C3 is completed.…”

Section: Discussionsupporting

confidence: 91%

Disulfide bridges in human complement component C3b

Dolmer

Sottrup‐Jensen

1993

FEBS Letters

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The disulfide bridges of human complement component C3b, derived from C3 by removal of the 77‐residue C3a, have been determined. The 10 bridges are Cys537‐Cys794, Cys605‐Cys640, Cys851‐Cys1491, Cys1079‐Cys1169, Cys1336‐Cys1467, Cys1367‐Cys1436, Cys1448‐Cys1489, Cys1496‐Cys1568, Cys1515‐Cys1639, and Cys1615‐Cys1624. Including the 3 bridges in C3a (Cys670‐Cys698, Cys672‐Cys705, and Cys685‐Cys706) previously determined by high‐resolution X‐ray crystallography [Hoppe‐Seyler's Z. Physiol. Chem. 361 (1980) 1389‐1399] all disulfide bridges of C3 are localized. C3 and the strongly related C4 and C5 are members of the α2‐macroglobulin superfamily. The predicted bridge patterns of C4 and C5 are discussed and compared with that of α2‐macroglobulin.

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Section: Discussionsupporting

confidence: 91%

Disulfide bridges in human complement component C3b

Dolmer

Sottrup‐Jensen

1993

FEBS Letters

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“…Amino acids were analyzed essentially according to Schaller et al (1989). Blotted enzyme was excised from the polyvinylidene difluoride membrane, and hydrolyzed at 100°C for 6 h in gas phase under vacuum with 6 M hydrochloric acid containing 0.1% (by vol.)…”

Section: Amino Sugar and Amino Acid Analysismentioning

confidence: 99%

Phosphatidylinositol‐glycan‐specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high‐density lipoproteins

Hoener

Brodbeck

1992

European Journal of Biochemistry

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Phosphatidylinositol (Ptd1ns)-glycan-specific phospholipase D was purified from bovine and human serum by phase separation in Triton X-114 and by chromatography on DEAE-cellulose, octylSepharose, concanavalin-A -Sepharose, and hydroxyapatite. The purification of the two enzymes was approximately 1200-fold with a recovery of 3-5%. Bovine serum contained about 40 pgglml of PtdIns-glycan-specific phospholipase D, about 10 times more than the amount determined in human serum. PtdIns-glycan-specific phospholipase D is also present in mammalian cerebrospinal fluid and in mammalian milk but to a much lesser extent than in serum. Enzyme from bovine and human serum displayed amphiphilic properties as revealed by sucrose density gradient centrifugation and gel filtration in the absence and presence of detergent. On density gradient centrifugation, both enzymes sedimented with an apparent sedimentation coefficient of about 6.0 S in the presence of 0.1% Triton X-100, and formed aggregates up to 14.5 S in the absence of detergent. Upon gel filtration, the bovine and human enzymes migrated with a Stokes' radius of 6.5 nm and 6.6 nm, respectively, in the presence of Triton X-100. In the absence of Triton X-100, both enzymes gave a Stokes' radius of 8.8 nm. Serial centrifugation of serum at increasing NaBr concentrations revealed that the majority of the enzyme is contained in the high-density lipoprotein fraction. PtdIns-glycanspecific phospholipase D from bovine and human serum contained 27 and 28 N-acetylglucosamine residues, respectively. Treatment with N-glycosidase F decreased the apparent molecular mass of the bovine and human enzyme from 115 and 123 kDa to 91 and 87 kDa, respectively. Sequence analysis of peptides derived from PtdIns-glycan-specific phospholipase D of bovine serum by CNBr cleavage gave 100% identity to the sequence published for the bovine liver enzyme while there was 83% similarity and 74% identity to the sequence of peptides obtained from the human serum enzyme.

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Identification of the disulfide bonds of the human complement component C3

Cited by 2 publications

References 6 publications

Disulfide bridges in human complement component C3b

Disulfide bridges in human complement component C3b

Phosphatidylinositol‐glycan‐specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high‐density lipoproteins

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