[A study of enzymatic hydrolysis of splenopentin and its analogs in human serum].
Degradation of immunoactive peptide splenopentin and its analogue N-acetylsplenopentin in human serum has been investigated by 1H NMR spectroscopy. It is shown that degradation of splenopentin occurs due to hydrolysis of peptide bonds in its N-terminal part, whereas in N-acetylsplenopentin peptide bonds in C-terminal part of the molecule are cleaved. Degradation pathways and life times of these peptides in human serum are established.
Isakova
O L
OL
Sepetov
N F
NF
Forner
K
K
Erlikh
A
A
D006801:Humans; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000097:blood / Q000378:metabolism*; D010455:Peptides; D013946:Thymopoietins / Q000097:blood / Q000378:metabolism*; D013951:Thymus Hormones / Q000378:metabolism*
D010446:Peptide Fragments; D010455:Peptides; D013946:Thymopoietins; D013951:Thymus Hormones; C060358:N-acetylsplenopeptin; C041898:splenopentin
Issledovanie fermentativnogo gidroliza splenopentina i ego analogov v syvorotke krovi chekloveka.