Results 261 to 270 of about 166,295 (311)

Tripeptidyl-peptidase II: A multi-purpose peptidase

International Journal of Biochemistry and Cell Biology, 2005
Tripeptidyl-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
exaly   +3 more sources

Equine peptidases: Correspondence with human peptidases and polymorphism for erythrocyte peptidase a

Biochemical Genetics, 1979
Equine 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
openaire   +2 more sources

‘Species’ of peptidases

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
openaire   +2 more sources

Peptidase in the cornea

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
openaire   +2 more sources

Signal Peptidases

ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel   +3 more
openaire   +2 more sources

Leader peptidase

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.
openaire   +2 more sources

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