Primary structure of Golfingia gouldii hemerythrin. Order of peptides in fragments produced by tryptic digestion of succinylated hemerythrin. Complete amino acid sequence

Biochemistry ◽  
1968 ◽  
Vol 7 (11) ◽  
pp. 3868-3878 ◽  
Author(s):  
Gerald L. Klippenstein ◽  
James W. Hollerman ◽  
Irving M. Klotz
1982 ◽  
Vol 207 (2) ◽  
pp. 253-260 ◽  
Author(s):  
M A Smith ◽  
L M Gerrie ◽  
B Dunbar ◽  
J E Fothergill

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.


1974 ◽  
Vol 27 (6) ◽  
pp. 591 ◽  
Author(s):  
RG Whittaker ◽  
EOP Thompson

Blood from the platypus contained three haemoglobins which were separated by chromatography on DEAE-Sephadex. The major component, Hb-I, was converted to globin and fractionated into the oc-and p-chains by chromatography on eM-cellulose in 8M urea-thiol buffers, and the complete amino acid sequence of the 141 residues of the oc-chain were determined. Peptides derived from the oc-chain by tryptic digestion were isolated by paper ionophoresis and chromatography. The amino acid sequences were determined by the dansyl-Edman procedure or by further digestion with other enzymes.


1979 ◽  
Vol 34 (9-10) ◽  
pp. 880-881 ◽  
Author(s):  
Gerhard Braunitzer ◽  
Jone Liberatori ◽  
Hans-Jürgen Kolde

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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