Amino acid composition and N-terminus of Pseudomonas cytochrome oxidase (= Pseudomas aerugenosa nitrite reductase)

1970 ◽  
Vol 221 (3) ◽  
pp. 668-671 ◽  
Author(s):  
Yoko Nagata ◽  
Tateo Yamanaka ◽  
Kazuo Okunuki
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Cytochrome Oxidase ◽  
Acid Composition ◽  
Nitrite Reductase ◽  
N Terminus

scholarly journals Association of purified skeletal-muscle AMP deaminase with a histidine–proline-rich-glycoprotein-like molecule

1997 ◽  
Vol 326 (3) ◽  
pp. 641-648 ◽  
Author(s):  
Maria RANIERI-RAGGI ◽  
Umberto MONTALI ◽  
Francesca RONCA ◽  
Antonietta SABBATINI ◽  
Paul E. BROWN ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Rabbit Skeletal Muscle ◽  
Striking Similarity ◽  
The Novel ◽  
Amp Deaminase ◽  
Rabbit Plasma ◽  
N Terminus

Denaturation of rabbit skeletal-muscle AMP deaminase in acidic medium followed by chromatography on DEAE-cellulose in 8 M urea at pH 8.0 allows separation of two main peptide components of similar apparent molecular mass (75–80 kDa) that we tentatively assume correspond to two different enzyme subunits. Whereas the amino acid composition of one of the two peptides is in good agreement with that derived from the nucleotide sequence of the known rat and human AMPD1 cDNAs, the second component shows much higher contents of proline, glycine and histidine. N-Terminal sequence analysis of the fragments liberated by limited proteolysis with trypsin of the novel peptide reveals a striking similarity to the fragments produced by plasmin cleavage of the rabbit plasma protein called histidine–proline-rich glycoprotein (HPRG). However, some divergence is observed between the sequence of one of the fragments liberated from AMP deaminase by a more extensive trypsinization and rabbit plasma HPRG in the region containing residues 472–477. A fragment with a blocked N-terminus, which was found among those liberated by proteolysis with pepsin of either whole AMP deaminase or the novel component of the enzyme, shows an amino acid composition quite different from that of the N-terminus of the known subunit of AMP deaminase. By coupling this observation with the detection in freshly prepared AMP deaminase of a low yield of the sequence (LTPTDX) corresponding to that of HPRG N-terminus, it can be deduced that in comparison with HPRG, the putative HPRG-like component of AMP deaminase contains an additional fragment with a blocked N-terminus, which is liberated by a proteolytic process during purification of the enzyme. The implications of the association to rabbit skeletal-muscle AMP deaminase of a HPRG-like protein species are discussed.

An analysis of amino acid composition of a few oxidoreductases by different methods

1983 ◽  
Vol 3 (3) ◽  
pp. 269-273
Author(s):  
Ali Naqui ◽  
Jean-Claude Vincent
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Cytochrome Oxidase ◽  
Acid Composition ◽  
And Function ◽  
Analyze Amino Acid

1. All methods used to analyze amino acid composition of different enzymes agree well with each other. 2. They lead to a relationship between amino acid composition and function of proteins. 3. Cytochrome oxidase is in a class by itself; copper-containing oxidases are closely related as expected.

Effect of maternal diet on the amino acid composition of human uterine fluid

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Maternal Diet ◽  
Uterine Fluid
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