Synthesis and characterization of poly(aspartic acid) derivatives conjugated with various amino acids

2010 ◽  
Vol 18 (5) ◽  
pp. 881-890 ◽  
Author(s):  
Ji-Heung Kim ◽  
Chang Mo Son ◽  
Young Sil Jeon ◽  
Woo-Seok Choe
1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.


1981 ◽  
Vol 13 (3) ◽  
pp. 367-378
Author(s):  
Kevin Bullock ◽  
Donald G. Davis ◽  
George G. Guilbault

Peptides 1994 ◽  
1995 ◽  
pp. 541-542
Author(s):  
H. Yamamoto ◽  
T. Nishina ◽  
N. Yumoto ◽  
T. Taguchi ◽  
Y. Tatsu ◽  
...  

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