Determination of the N-terminal sequence and amino acid composition of MM and BB isozymes of porcine creatine phosphokinase

1988 ◽  
Vol 106 (3) ◽  
pp. 1250-1252
Author(s):  
F. E. Romantsev ◽  
V. N. Prozorovskii ◽  
A. A. Rzhaninova ◽  
E. L. Trebukhina
1959 ◽  
Vol 234 (5) ◽  
pp. 1108-1111
Author(s):  
Bo G. Malmström ◽  
J.R. Kimmel ◽  
Emil L. Smith

1978 ◽  
Vol 253 (4) ◽  
pp. 1305-1314
Author(s):  
J.C. Regier ◽  
F.C. Kafatos ◽  
K.J. Kramer ◽  
R.L. Heinrikson ◽  
P.S. Keim

1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.


1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.


1964 ◽  
Vol 17 (4) ◽  
pp. 283-285
Author(s):  
Takao Shinagawa ◽  
Toshio Habu ◽  
Akemi Murakami

2019 ◽  
Vol 18 (1) ◽  
pp. 85-91
Author(s):  
AI Kriukova ◽  
IM Vladymyrova ◽  
OL Levashova ◽  
TS Tishakova

The amino acid composition of the roots of Harpagophytum procumbens was investigated by the method of high performance liquid chromatography (HPLC) with preliminary derivatization. Sixteen free and thirteen bound amino acids were quantitatively determined. The content of protein-bound amino acids was calculated. Dhaka Univ. J. Pharm. Sci. 18(1): 85-91, 2019 (June)


2020 ◽  
Vol 58 (8) ◽  
pp. 687-694
Author(s):  
Kumarswamy Ummiti ◽  
J V Shanmukha Kumar

Abstract Ganirelix is a synthetic decapeptide linked with nine different amino acids. To understand the peptide amino acid sequence or primary structure, the first step is to determine the amino acid composition of the peptide which can be a determining factor for the peptide immunogenicity. Edman degradation is not a suitable analytical technique to identify amino acid sequence present in Ganirelix due to the absence of uncharged N-terminal amino group. To address this challenge, a pre-column derivatization method was developed with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent. In the present work, the Ganirelix active pharmaceutical ingredient present in the injectable formulation was isolated by fraction collection and further purified by flash chromatography. The amino acid composition of Ganirelix is assayed by carrying out acid hydrolysis with 6 mol L−1 hydrochloric acid solution containing 1% phenol at 100°C for 24 h and derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent solution, followed by determination of individual amino acids by reverse-phase chromatography using a C18 column. High resolution was achieved for the nine amino acid mixture. The amino acid composition results of temperature-stressed Ganirelix generic product and reference listed drug are in good agreement with the theoretical molar ratio of label information.


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