The N-domain of angiotensin-converting enzyme specifically hydrolyzes the Arg-5-His-6 bond of Alzheimer's Aβ-(1-16) peptide and its isoAsp-7 analogue with different efficiency as evidenced by quantitative matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Rapid Communications in Mass Spectrometry

Volumn 22, Issue 2, 2008, Pages 231-239

  Toropygin, Ilya Yu ^a   Kugaevskaya, Elena V ^a   Mirgorodskaya, Olga A ^b   Elisseeva, Yulia E ^a   Kozmin, Yuri P ^c   Popov, Igor A ^a   Nikolaev, Eugene N ^a   Makarov, Alexander A ^d   Kozin, Sergey A ^a  

^a INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

^b INSTITUTE FOR ANALYTICAL INSTRUMENTATION   (Russian Federation)

^c SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^d ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

DESORPTION; ENZYMES; HYDROLYSIS; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES;

ALZHEIMER; ALZHEIMERS DISEASE; AMYLOID-BETA PEPTIDES; ANGIOTENSIN-CONVERTING ENZYME; C-DOMAIN; HOMOEOSTASIS; IN-VITRO; MATRIX-ASSISTED LASER DESORPTION/IONIZATION-TIME-OF-FLIGHT MASS SPECTROMETRY; POST-TRANSLATIONAL MODIFICATIONS; QUANTITATIVE MATRICES;

PEPTIDES;

EID: 38549117383     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.3357     Document Type: Article

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