Purification and characterization of a human kidney neutral endopeptidase that hydrolyzes succinyl trialanine-4-nitroanilide and biologically active peptides

Sea urchin gonads have been demonstrated to contain major yolk protein (MYP), which can be hydrolyzed by enzymes to release biologically active peptides.

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Online SERS detection and characterization of eight biologically-active peptides separated by capillary zone electrophoresis

The Analyst ◽

10.1039/c4an01980f ◽

2015 ◽

Vol 140 (5) ◽

pp. 1516-1522 ◽

Cited By ~ 20

Author(s):

Pierre Negri ◽

Scott A. Sarver ◽

Nicole M. Schiavone ◽

Norman J. Dovichi ◽

Zachary D. Schultz

Keyword(s):

Low Cost ◽

Biologically Active ◽

Sheath Flow ◽

Active Peptides ◽

Biologically Active Peptides ◽

Zone Electrophoresis ◽

Sers Detection ◽

Capillary Zone ◽

Specific Detector

Sheath-flow SERS provides a low cost, sensitive and chemical specific detector for routine characterization of biomolecules following a CZE separation.

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Emerging Family of Proline-Specific Peptidases ofPorphyromonas gingivalis: Purification and Characterization of Serine Dipeptidyl Peptidase, a Structural and Functional Homologue of Mammalian Prolyl Dipeptidyl Peptidase IV

Infection and Immunity ◽

10.1128/iai.68.3.1176-1182.2000 ◽

2000 ◽

Vol 68 (3) ◽

pp. 1176-1182 ◽

Cited By ~ 37

Author(s):

Agnieszka Banbula ◽

Marcin Bugno ◽

Jason Goldstein ◽

Jane Yen ◽

Daniel Nelson ◽

...

Keyword(s):

Defense Mechanisms ◽

Single Copy ◽

Dipeptidyl Peptidase ◽

Biochemical Properties ◽

Dipeptidyl Peptidase Iv ◽

Biologically Active ◽

Purification And Characterization ◽

Inhibitory Peptide ◽

Active Peptides

ABSTRACT Porphyromonas gingivalis is an asaccharolytic and anaerobic bacterium that possesses a complex proteolytic system which is essential for its growth and evasion of host defense mechanisms. In this report, we show the purification and characterization of prolyl dipeptidyl peptidase IV (DPPIV) produced by this organism. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated. P. gingivalis DPPIV, like its human counterpart, is able to cleave the N terminus of synthetic oligopeptides with sequences analogous to those of interleukins 1β and 2. Additionally, this protease hydrolyzes biologically active peptides including substance P, fibrin inhibitory peptide, and β-casomorphin. Southern blot analysis of genomic DNA isolated from several P. gingivalis strains reveal that a single copy of the DPPIV gene was present in all strains tested.

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Exploring the structure and function of zinc metallopeptidases: old enzymes and new discoveries

Biochemical Society Transactions ◽

10.1042/bst0310723 ◽

2003 ◽

Vol 31 (3) ◽

pp. 723-727 ◽

Cited By ~ 63

Author(s):

A.J. Turner

Keyword(s):

Neutral Endopeptidase ◽

Biologically Active ◽

Amyloid Peptide ◽

Active Peptides ◽

Catalytic Sites ◽

Biologically Active Peptides ◽

Neuroprotective Actions ◽

And Function ◽

Insight Into ◽

Physiological Substrates

Neprilysin [or neutral endopeptidase (NEP)] and angiotensin-converting enzyme (ACE) are zinc metallopeptidases involved in the extracellular metabolism of biologically active peptides. Recent genomic advances have led to the identification of novel homologues of each of these ectoenzymes and new physiological and pathological roles are emerging for them. The structures of each of these peptidases have recently been solved providing insight into their distinct catalytic sites. In addition to its originally identified role in neuropeptide metabolism in the nervous system, NEP is implicated in regulation of the cardiovascular system and is protective in prostate and certain other cancers. Hence the cellular concentration of NEP is critical to tissue homoeostasis. Most recently, NEP has been shown to exert neuroprotective actions, principally through its ability to catabolize the neurotoxic Alzheimer's amyloid peptide. The only known homologue of ACE, termed ACE2, is critical to cardiovascular function, but its physiological substrates and precise metabolic roles remain to be elucidated. Other members of these growing metallopeptidase families await further characterization and possible exploitation as therapeutic targets.

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