CORRECTION. The Amino Acid Sequence at the Catalytic Site of Phosoglucomutase from Rabbit Muscle*

Biochemistry ◽  
1966 ◽  
Vol 5 (2) ◽  
pp. 811-811
Author(s):  
Sidney Harshman ◽  
Victor Najjar
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Site ◽  
Rabbit Muscle

The Amino Acid Sequence at the Catalytic Site of Phosphoglucomutase from Rabbit Muscle*

Biochemistry ◽  
1965 ◽  
Vol 4 (11) ◽  
pp. 2526-2535 ◽  
Author(s):  
Sidney Harshman ◽  
Victor A. Najjar
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Site ◽  
Rabbit Muscle

scholarly journals Amino Acid Sequence Around the Catalytic Site in Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus

1972 ◽  
Vol 111 (3) ◽  
pp. 797-800 ◽  
Author(s):  
J. Bridgen ◽  
J. I. Harris ◽  
P. W. McDonald ◽  
R. E. Amelunxen ◽  
J. R. Kimmel
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bacillus Stearothermophilus ◽  
Catalytic Site

The Amino Acid Sequence of the N-Terminal Region of Aldolase

1973 ◽  
Vol 51 (5) ◽  
pp. 514-519 ◽  
Author(s):  
P. J. Anderson ◽  
D. Gibson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Terminal Region ◽  
Rabbit Muscle

The amino acid sequence of the N-terminal 39 residues of sturgeon muscle aldolase has been determined by a combination of automated and manual sequencing procedures. In addition, the sequence of the N-terminal 19 residues of rabbit muscle aldolase has been determined using a sequenator. It was apparent from these studies that aldolase primary structure is highly conserved in this region.

scholarly journals The complete amino acid sequence of rabbit muscle phosphoglucomutase.

1983 ◽  
Vol 258 (15) ◽  
pp. 9166-9174 ◽  
Author(s):  
W J Ray ◽  
M A Hermodson ◽  
J M Puvathingal ◽  
W C Mahoney
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rabbit Muscle ◽  
Complete Amino Acid Sequence

scholarly journals Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle

1974 ◽  
Vol 139 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Anna J. Furth ◽  
J. D. Milman ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Rabbit Muscle ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Triose Phosphate

1. Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH4)2SO4 fraction of an extract of homogenized chicken breast muscle. The product is homogeneous on gel electrophoresis and is suitable for growing crystals for X-ray work. The specific activity is 10000 units/mg and the value for E0.1%280 is 1.20. 2. Comparison between the sum of the amino acid compositions of the tryptic peptides of the protein and the amino acid composition obtained on total hydrolysis of the protein indicates that the relative subunit mass is about 27000. 3. These data, together with the results of the examination of the amino acid compositions of a number of minor peptides, the number of peptides in the tryptic digest and the complete amino acid sequences of the tryptic peptides (the determination of which is described here), give no indication that the subunits are dissimilar. 4. A tentative amino acid sequence is presented for the protein, in which the ordering of the tryptic peptides is derived by homology with the sequence of the rabbit muscle enzyme (Corran & Waley, 1973). 5. An appendix describes the use that was made of mass spectrometry in the determination of some of the sequences. Mass-spectrometric data have been obtained for 35 residues, that is about 15% of the total sequence of the protein. 6. An extended version of the present paper has been deposited as Supplementary Publication SUP 50025 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

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