Results 201 to 210 of about 149,172 (264)
Development and structure-guided characterization of a novel ACE2-binding macrocyclic peptide. [PDF]
J Struct Biol XBenoit RM +9 more
europepmc +1 more source
The Caenorhabditis elegans DPF-3 and human DPP4 have tripeptidyl peptidase activity. [PDF]
FEBS LettTrivedi A, Gudipati RK.
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Lobeglitazone and the risk of renal progression in Korean patients with type 2 diabetes mellitus: a retrospective cohort study. [PDF]
BMJ OpenHong SH +7 more
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Tripeptidyl-peptidase II: A multi-purpose peptidase
The International Journal of Biochemistry & Cell Biology, 2005Tripeptidyl-peptidase II is a high-molecular weight peptidase with a widespread distribution in eukaryotic cells. The enzyme sequentially removes tripeptides from a free N-terminus of longer peptides and also displays a low endopeptidase activity. A role for tripeptidyl-peptidase II in the formation of peptides for antigen presentation has recently ...
Birgitta, Tomkinson +1 more
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Equine peptidases: Correspondence with human peptidases and polymorphism for erythrocyte peptidase a
Biochemical Genetics, 1979Equine erythrocyte peptidases were compared to the six human erythrocyte peptidases, A, B, C, D, E, and F, regarding substrate specificity, relative activity, and electrophoretic mobility. Five equine erythrocyte peptidases appeared homologous to human peptidases A, B, D, E, and F.
J, Yut, L R, Weitkamp
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bchm, 2007
Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
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Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
openaire +2 more sources
Experimental Eye Research, 1969
Peptidase activity, operative at neutral pH, was found in bovine cornea and conjunctiva with a synthetic substrate assay. The same peptidase was found previously in commercial bacterial collagenase preparations. Cell fractionation of homogenates revealed the activity to be maximal in the high-speed supernatant of the corneal and conjunctival epithelium,
H H, Slansky +4 more
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Peptidase activity, operative at neutral pH, was found in bovine cornea and conjunctiva with a synthetic substrate assay. The same peptidase was found previously in commercial bacterial collagenase preparations. Cell fractionation of homogenates revealed the activity to be maximal in the high-speed supernatant of the corneal and conjunctival epithelium,
H H, Slansky +4 more
openaire +2 more sources
ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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Chorionic peptidase inactivates GnRH as a post‐proline peptidase
International Journal of Gynecology & Obstetrics, 1992Recently, we have described a chorionic peptidase (C-ase-1) which inactivates gonadotropin releasing hormone (GnRH), oxytocin, angiotensin II and thyrotropin releasing hormone. Since all these hormones contain a proline residue, we proposed that C-ase-1 may act as a post-proline peptidase.
I S, Kang, T M, Siler-Khodr
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