study of a new and specific proline cleaving peptidase from bovine serum.
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study of a new and specific proline cleaving peptidase from bovine serum. by Patrick J. Collins

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Published .
Written in English


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Thesis (PhD) -- Dublin City University, 2003.

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Open LibraryOL21993949M

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Due to its complete insensitivity towards the classic prolyl oligopeptidase inhibitor Z-Pro-prolinal, this peptidase was designated Z-Proprolinal Insensitive Peptidase (ZIP). The study o f this new and specific proline cleaving endopeptidase from bovine serum is : Patrick Collins.   4. Proline specific peptidases. The particular conformational and biochemical attributes conferred upon a peptide by the presence of proline, will influence its interaction with other proteins, including enzymes. Such a restriction on the susceptibility of polypeptides to proteolytic hydrolysis, offers a mechanism of protection against by:   The study of a new proline-specific peptidase from bovine serum is presented. The enzyme readily cleaves the prolyl oligopeptidase (PO) substrate Z-Gly-Pro-MCA, liberating the fluorophore MCA, thus allowing quantification of enzyme by:   Proline-specific dipeptidyl peptidase-like (DPP IV; EC ) activity in bovine serum has attracted little attention despite its ready availability and the paucity of useful proline-cleaving enzymes. Bovine serum DPP IV-like peptidase is very tolerant of organic solvents, particularly acetonitrile: upon incubation for 1 h at room.

Proline-specific peptidases (PsP) belong to different families of hydrolases acting on peptide bonds (EC x.x). They occur in various organisms including bacteria, fungi, plants and insects. The endopeptidase, post-proline cleaving enzyme, has been puriffold in an overall yield of 18% from lamb kidney. The enzyme possesses a specific activity of 45 ~mol/mg/min as tested with the substrate Z-Gly-Pro-Leu-Gly (K,,, = x 10m5), has a molecular weight of ,, is comprised. The study of a new proline-specific peptidase from bovine serum is presented. The enzyme readily cleaves the prolyl oligopeptidase (PO) substrate Z-Gly-Pro-MCA, liberating the fluorophore MCA. Two post-proline cleaving peptidases PPCP1 and PPCP2 with molecular masses of and 63 kDa, respectively, hydrolyzing Z-AlaAlaPro-pNA were isolated for the first time from the larval midgut of the yellow mealworm Tenebrio molitor and characterized. PPCP1 was active only in acidic media, with a maximum at pH , whereas PPCP2, both in acidic and alkaline media with a maximum at pH

The discovery of a potentially novel proline-specific peptidase from bovine serum is presented which is capable of cleaving the dipeptidyl peptidase IV (DPIV) substrate Gly-Pro-MCA. The enzyme was isolated and purified with the use of Phenyl Sepharose Hydrophobic Interaction, Sephacryl S Gel Filtration, and Q-Sephacryl Anion Exchange. Collins, Patrick () The study of a new and specific proline cleaving peptidase from bovine serum. PhD thesis, Dublin City University. Colleary, Sandra () The use of chemically stabilised proteolytic enzymes in peptide synthesis. PhD thesis, Dublin City University. Proline-specific dipeptidyl peptidase-like (DPP IV; EC ) activity in bovine serum has attracted little attention despite its ready availability and the paucity of useful proline-cleaving.   Cunningham and O’Connor (b) reported the first observation of a second Z-Gly-Pro-AMC hydrolysing activity in bovine serum. The uniqueness of this peptidase was its ability to cleave the specific prolyl oligopeptidase fluorogenic substrate Z-Gly-Pro-AMC, but being completely distinct to this serine protease (Birney & O’Connor,