scholarly journals Purification and Characterization of Dipeptidyl Aminopeptidase fromAureobacteriumsp. WO26

1997 ◽  
Vol 61 (1) ◽  
pp. 146-151 ◽  
Author(s):  
Wataru Ogasawara ◽  
Noriyuki Inanobe ◽  
Keiko Ochiai ◽  
Katsuhiko Ando ◽  
Hirofumi Okada ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Dipeptidyl Aminopeptidase

Purification and characterization of x-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris NRRL 634

2006 ◽  
Vol 22 (9) ◽  
pp. 953-958 ◽  
Author(s):  
Alfredo E. Pérez-Guzmán ◽  
Teresa Cruz y Victoria ◽  
Ramón Cruz-Camarillo ◽  
Humberto Hernández-Sánchez
Keyword(s):  
Lactococcus Lactis ◽  
Purification And Characterization ◽  
Lactococcus Lactis Subsp ◽  
Dipeptidyl Aminopeptidase

Purification and characterization of a post-proline dipeptidyl aminopeptidase fromStreptococcus cremorisAM2

1990 ◽  
Vol 57 (1) ◽  
pp. 89-99 ◽  
Author(s):  
Mary Booth ◽  
Ide Ni Fhaoláin ◽  
P. Vincent Jennings ◽  
Gerard O'Cuinn
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Cheese Ripening ◽  
Streptococcus Cremoris ◽  
Scissile Bond ◽  
Dipeptidyl Aminopeptidase

SummaryThe present study describes the purification of a post-proline dipeptidyl aminopeptidase from the cytoplasm ofStreptococcus cremorisAM2. On the basis of its elution from a calibrated Sephadex G200 column, the enzyme had a molecular weight of 117000 and exhibited a broad pH optimum activity between 6·0 and 9·0. The activity was most comprehensively inhibited by phenylmethylsulphonylfluoride and more modestly inhibited by 1,10-phenanthroline and 8-hydroxyquinoline but not by EDTA. A range of peptides containing either proline or alanine as the penultimate amino acid residue could act as substrates. The presence of proline on the carboxy side of the scissile bond prevented hydrolysis. However the enzyme could release Pro-Pro from Pro-Pro-Gly-Phe-Ser-Pro. The significance of this substrate specificity is considered in the context of removal of either single proline residues or prolylproline sequences from oligopeptides during cheese ripening.

Partial purification and characterization of dipeptidyl-aminopeptidase III fromDictyostelium discoideum

1987 ◽  
Vol 11 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Samuel A.T. Chan ◽  
Theodore H.D. Jones ◽  
John P. Sweeney ◽  
Karim Toursarkissian
Keyword(s):  
Partial Purification ◽  
Purification And Characterization ◽  
Dipeptidyl Aminopeptidase

scholarly journals Purification and characterization of the X-prolyl-dipeptidyl aminopeptidase (PepX) from Streptococcus macedonicus and cloning of the pepX gene

2002 ◽  
Vol 82 (6) ◽  
pp. 657-671 ◽  
Author(s):  
Marina D. Georgalaki ◽  
Marina Papdelli ◽  
Rania Anastasiou ◽  
George Kalantzopoulos ◽  
Effie Tsakalidou
Keyword(s):  
Purification And Characterization ◽  
Dipeptidyl Aminopeptidase

scholarly journals Purification and characterization of dipeptidyl aminopeptidase III from human placenta.

1986 ◽  
Vol 34 (8) ◽  
pp. 3333-3340 ◽  
Author(s):  
YOSHIMITU SHIMAMORI ◽  
YASUHIRO WATANABE ◽  
YUKIO FUJIMOTO
Keyword(s):  
Human Placenta ◽  
Purification And Characterization ◽  
Dipeptidyl Aminopeptidase
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