scholarly journals Characterization of the B-chain of human plasma alpha 2HS-glycoprotein. The complete amino acid sequence and primary structure of its heteroglycan.

1983 ◽  
Vol 258 (8) ◽  
pp. 4966-4971 ◽  
Author(s):  
F Gejyo ◽  
J L Chang ◽  
W Bürgi ◽  
K Schmid ◽  
G D Offner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Plasma ◽  
Primary Structure ◽  
Complete Amino Acid Sequence

scholarly journals Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequence

1982 ◽  
Vol 207 (2) ◽  
pp. 253-260 ◽  
Author(s):  
M A Smith ◽  
L M Gerrie ◽  
B Dunbar ◽  
J E Fothergill
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Gel Filtration ◽  
Complete Amino Acid Sequence ◽  
The Third ◽  
Human Sequence ◽  
Bovine Plasma ◽  
Bovine Sequence ◽  
C 50

Purification of C4a from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a has been determined by automatic sequencer degradation of CNBr and enzymic fragments, and by carboxypeptidase digestion. The 77-residue bovine sequence shows 12 differences from the human sequence with five of these differences occurring in the C-terminal 11 residues. The sequence of C4a confirms earlier suggestions of homology with C3a and C5a: the three sequences show an almost equal number of identities with each other. The six cysteine residues of the ‘disulphide knot’ are conserved as well as seven other residues including the C-terminal arginine.

The Primary Structure of the β-Lactoglobulin of the Waterbuffalo (Bubalus arnee)

1979 ◽  
Vol 34 (9-10) ◽  
pp. 880-881 ◽  
Author(s):  
Gerhard Braunitzer ◽  
Jone Liberatori ◽  
Hans-Jürgen Kolde
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Complete Amino Acid Sequence ◽  
Β Lactoglobulin

Abstract The complete amino acid sequence of the β-lactoglobuline of the waterbuffalo (Bubalus arnee) was established. The sequence of peptides obtained by cleavage with BNPS-Skatole, CNBr and trypsin were determined automatically by the help of the sequenator. Only two differences were found in the β-lactoglobulin of the waterbuffalo compared with the bovine β-lactoglobulin B.

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