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Screening, Safety Assessment, and Process Optimization of Lactic Acid Bacteria from Traditional Yak Yogurt as Adjunct Cultures. [PDF]
Shuang W +5 more
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The Caenorhabditis elegans DPF-3 and human DPP4 have tripeptidyl peptidase activity. [PDF]
Trivedi A, Gudipati RK.
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Tripeptidyl-peptidase II: A multi-purpose peptidase
International Journal of Biochemistry and 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
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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
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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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Molecular Microbiology, 1991
SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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