scholarly journals Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases

1997 ◽  
Vol 327 (1) ◽  
pp. 199-202 ◽  
Author(s):  
Karen L. LEE ◽  
Karen L. ALBEE ◽  
Richard J. BERNASCONI ◽  
Tim EDMUNDS
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cysteine Proteases ◽  
Egg White ◽  
Amino Acid Sequences ◽  
Cysteine Protease Inhibitors ◽  
Peptide Substrates ◽  
Complete Amino Acid Sequence ◽  
Theoretical Mass ◽  
Stem Bromelain

The amino acid sequences of ananain (EC 3.4.22.31) and stem bromelain (3.4.22.32), two cysteine proteases from pineapple stem, are similar yet ananain and stem bromelain possess distinct specificities towards synthetic peptide substrates and different reactivities towards the cysteine protease inhibitors E-64 and chicken egg white cystatin. We present here the complete amino acid sequence of ananain and compare it with the reported sequences of pineapple stem bromelain, papain and chymopapain from papaya and actinidin from kiwifruit. Ananain is comprised of 216 residues with a theoretical mass of 23464 Da. This primary structure includes a sequence insert between residues 170 and 174 not present in stem bromelain or papain and a hydrophobic series of amino acids adjacent to His-157. It is possible that these sequence differences contribute to the different substrate and inhibitor specificities exhibited by ananain and stem bromelain.

scholarly journals Studies on Monotreme Proteins. V. Amino Acid Sequence of the a-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

1974 ◽  
Vol 27 (6) ◽  
pp. 591 ◽  
Author(s):  
RG Whittaker ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Complete Amino Acid Sequence ◽  
Ornithorhynchus Anatinus ◽  
A Chain

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.

scholarly journals Complete amino acid sequence of cyanobacterial gas-vesicle protein indicates a 70-residue molecule that corresponds in size to the crystallographic unit cell

1986 ◽  
Vol 236 (1) ◽  
pp. 31-36 ◽  
Author(s):  
P K Hayes ◽  
A E Walsby ◽  
J E Walker
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Electrophoretic Analysis ◽  
Amino Acid Sequences ◽  
Unit Cell ◽  
Gas Vesicles ◽  
Complete Amino Acid Sequence ◽  
X Ray Crystallography ◽  
Beta Sheet Structure ◽  
Vesicle Protein

Gas vesicles of cyanobacteria are formed by a protein called ‘gas-vesicle protein’ (GVP). The complete amino acid sequence has been determined of GVP from Anabaena flos-aquae. It is 70 residues long and has an Mr of 7388. This corresponds to the size of the repeating unit cell demonstrated by X-ray crystallography of intact gas vesicles. Details of the sequence are related to the secondary beta-sheet structure of the protein and its contrasting hydrophilic and hydrophobic surfaces. Extensive amino acid sequences have also been determined for GVPs from two other cyanobacteria, species of Calothrix and Microcystis; they are highly homologous with that of Anabaena GVP. Electrophoretic analysis indicates that GVPs of different cyanobacteria form a variety of stable oligomers.

The Complete Amino Acid Sequence of Green Turtle (Chelonia mydas) Egg White Ribonuclease

2006 ◽  
Vol 25 (5) ◽  
pp. 316-327 ◽  
Author(s):  
Somporn Katekaew ◽  
Takao Torikata ◽  
Tomohiro Araki
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Green Turtle ◽  
Chelonia Mydas ◽  
Egg White ◽  
Complete Amino Acid Sequence

scholarly journals The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain

1970 ◽  
Vol 117 (2) ◽  
pp. 341-346 ◽  
Author(s):  
S. S. Husain ◽  
G. Lowe
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sodium Borohydride ◽  
Active Site ◽  
Iodoacetic Acid ◽  
Amino Acid Sequences ◽  
Histidine Residues ◽  
Active Site Cysteine ◽  
Stem Bromelain ◽  
High Degree

Stem bromelain that had been irreversibly inhibited with 1,3-dibromo[2-14C]-acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and α-chymotrypsin three radioactive peptides were isolated chromatographically. The amino acid sequences around the cross-linked cysteine and histidine residues were determined and showed a high degree of homology with those around the active-site cysteine and histidine residues of papain and ficin.

scholarly journals Studies on Marsupial Proteins IV. Amino Acid Sequence of Myoglobin From the Red Kangaroo, Megaleia Rufa

1971 ◽  
Vol 24 (1) ◽  
pp. 75 ◽  
Author(s):  
GM Air ◽  
EOP Thompson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Single Component ◽  
Amino Acid Residues ◽  
Histidine Residues ◽  
Complete Amino Acid Sequence ◽  
Red Kangaroo

Myoglobin isolated from skeletal muscle of M. rufa consists of a single component containing 153 amino acid residues. The complete amino acid sequence has been determined. Oleavage with cyanogen bromide gave four polypeptides which were further fragmented by digestion with trypsin or chymotrypsin. The amino acid sequences of the peptides obtained were determined by the "dansyl"-Edman procedure. The order of the cyanogen bromide fragments was readily deduced from terminal sequences. Digestion of maleylated myoglobin with trypsin and cleavage at histidine residues with N-bromosuccinimide gave some overlapping sequences. Amino acid sequences in myoglobins are more conservative than in the ,B-chains of haemoglobin previously studied (Air and Thompson 1969) but the red kangaroo myoglobin shows more variation in amino acid sequence than has been found in myoglobins from other species.

Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan

Biochemistry ◽  
1980 ◽  
Vol 19 (9) ◽  
pp. 1814-1819 ◽  
Author(s):  
Richard J. Simpson ◽  
Geoffrey S. Begg ◽  
Donna S. Dorow ◽  
Francis J. Morgan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Egg White ◽  
Black Swan ◽  
Complete Amino Acid Sequence
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