AbstractWe have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences. The deduced amino acid sequence from the human clone showed sequence identity to both the α and β subunits of the rat enzyme. The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx. 19.5 (α) and 15 (β) kDa. A charge enriched region is present at the predicted site where cleavage occurs. Using polyclonal antibodies against the α and β subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme
The structural and functional characterization of human enzymes that are of potential medical and th...
Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. Bacteri...
AbstractA full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein ph...
AbstractWe have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using ...
Glycosylasparaginase (GA; EC 3.5.1.26) is a lysosomal enzyme that cleaves the N-glycosidic bond betw...
AbstractThe gene structure of the human lysosomal enzyme glycosylasparaginase was determined. The ge...
The apparent active site of human leukocyte gly-coasparaginase (N4-(~-acetylglucosaminy~)-~-aspa-rag...
AbstractGlycosylasparaginase is a lysosomal amidase involved in the degradation of glycoproteins. Re...
AbstractAspartylglucosaminuria (AGU, McKusick 208400) is an autosomal recessive lysosomal storage di...
The deamination of L-asparagine to L-aspartic acid and ammonia is catalyzed by L-asparaginases (L-as...
A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatas...
Aspartylglucosaminidase (AGA) is a lysosomal hydrolase that participates in the breakdown of glycopr...
L-asparaginases hydrolyze L-asparagine to L-aspartic acid and ammonia. Enzymes of bacterial origin a...
The asialoglycoprotein receptor (ASGPR) was the first described mammalian lectin that mediates the s...
Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. Bacteri...
The structural and functional characterization of human enzymes that are of potential medical and th...
Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. Bacteri...
AbstractA full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein ph...
AbstractWe have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using ...
Glycosylasparaginase (GA; EC 3.5.1.26) is a lysosomal enzyme that cleaves the N-glycosidic bond betw...
AbstractThe gene structure of the human lysosomal enzyme glycosylasparaginase was determined. The ge...
The apparent active site of human leukocyte gly-coasparaginase (N4-(~-acetylglucosaminy~)-~-aspa-rag...
AbstractGlycosylasparaginase is a lysosomal amidase involved in the degradation of glycoproteins. Re...
AbstractAspartylglucosaminuria (AGU, McKusick 208400) is an autosomal recessive lysosomal storage di...
The deamination of L-asparagine to L-aspartic acid and ammonia is catalyzed by L-asparaginases (L-as...
A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatas...
Aspartylglucosaminidase (AGA) is a lysosomal hydrolase that participates in the breakdown of glycopr...
L-asparaginases hydrolyze L-asparagine to L-aspartic acid and ammonia. Enzymes of bacterial origin a...
The asialoglycoprotein receptor (ASGPR) was the first described mammalian lectin that mediates the s...
Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. Bacteri...
The structural and functional characterization of human enzymes that are of potential medical and th...
Asparaginases catalyze the hydrolysis of the amino acid asparagine to aspartate and ammonia. Bacteri...
AbstractA full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein ph...