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aminoacyl-histidine dipeptidase

Known as: carnosinase, homocarnosinase 
 
National Institutes of Health

Papers overview

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Highly Cited
2010
Highly Cited
2010
Carnosine is found in high concentrations in skeletal muscles, where it is involved in several physiological functions. The… Expand
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Highly Cited
2009
Highly Cited
2009
Carnosine (beta-alanyl-L-histidine) is present in high concentrations in human skeletal muscles. The oral ingestion of beta… Expand
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Highly Cited
2007
Highly Cited
2007
OBJECTIVE—Carnosinase 1 (CN1) is a secreted dipeptidase that hydrolyzes l-carnosine. Recently, we have identified an allelic… Expand
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Highly Cited
2005
Highly Cited
2005
The risk of diabetic nephropathy is partially genetically determined. Diabetic nephropathy is linked to a gene locus on… Expand
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Highly Cited
2003
Highly Cited
2003
Carnosine (β-alanyl-l-histidine) and homocarnosine (γ-aminobutyric acid-l-histidine) are two naturally occurring dipeptides with… Expand
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Highly Cited
2000
Highly Cited
2000
Comparative study of hydrolysis of carnosine and a number of its natural derivatives by human serum and rat kidney carnosinase… Expand
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Highly Cited
1991
Highly Cited
1991
Carnosinase from human plasma was purified 18,000-fold to apparent homogeneity in a four step procedure. The dipeptidase was… Expand
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Highly Cited
1985
Highly Cited
1985
Human tissue carnosinase (EC 3.4.13.3) had optimum activity at pH9.5 and was a cysteine peptidase, being activated by… Expand
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Highly Cited
1982
Highly Cited
1982
Human serum carnosinase was assayed using a simple and sensitive fluorometric method. Under optimum conditions, the average adult… Expand
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Highly Cited
1979
Highly Cited
1979
Homocarnosine (HCarn) content varied over a 6‐fold range in different regions of autopsied human brain, being highest in the… Expand
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