About: Alanyl Aminopeptidase from Human Seminal Plasma: Purification, Characterization, and Immunohistochemical Localization in the Male Genital Tract(1)

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About: Alanyl Aminopeptidase from Human Seminal Plasma: Purification, Characterization, and Immunohistochemical Localization in the Male Genital Tract(1) Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Alanyl Aminopeptidase from Human Seminal Plasma: Purification, Characterization, and Immunohistochemical Localization in the Male Genital Tract(1)
Creator	Huang, Kai Ishida, Tetsuo Kinouchi, Toshiaki Nishi, Katsuji Ohkubo, Takahara, Shuji Takeyama, Masami Ueyama, Hisao
source	PMC
abstract	Alanyl aminopeptidase (AAP) was purified to homogeneity from human seminal plasma. The calculated molecular weight of the purified enzyme was approximately 137,000±5,000 from light scattering, 140,000 (main) and 137,000 (minor) from non-denatured PAGE and 153,000 from SDS-PAGE in the absence or presence of 2-mercaptoethanol (2-ME). These findings suggest that the enzyme is monomeric in form in human seminal plasma. The enzyme hydrolyzed several amino acid 4-methyl-coumaryl-7-amide (MCA) substrates. The order of K(cat;)/K(m) values of AAP at optimal pH (pH 7.5) was Ala- >Lys-Ala- ≥ Met- > Leu- > Phe- > Arg- ≥ Arg-Arg- > Lys- > Gly-MCAs. AAP was potently inhibited by bestatin, leuhis-tin, actinonin, amastatin, and 1,10-phenanthroline. These findings suggest that AAP is an aminopeptidase. We determined that the amino acid sequence of the first 22 residues of the enzyme was Ser(1)-Thr-Thr-Pro-Ser(5)-Ala-Ser-Ala-Thr-Thr(10)-Asn-Pro-Ala-Ser-Ala(15)-Thr-Thr-Leu-Asp-Gln(20)-Ser-Lys-. This sequence was completely coincident with that downstream of the transmembrane site of human intestinal alanyl aminopeptidase N (CD13). We also isolated cDNA encoding AAP from human prostate cDNA library, sequenced its structure, and confirmed human seminal plasma AAP to be identical with alanyl aminopeptidase N. We postulated that native human seminal plasma alanyl aminopeptidase is released into the seminal plasma after the specific site is cleaved by elastase or an elastase-like enzyme. The enzyme level in human seminal plasma determined by single radial immunodiffusion was 5.2±3.2mg/100ml (mean±SD, n=20) in individuals 20–47 years of age. AAP was immunohistochemically stained in the luminal site-cell membrane of epithelial cells in the prostatic gland and ductuli efferentes of the testis.
has issue date	1997-10-01(xsd:dateTime)
bibo:doi	10.1093/oxfordjournals.jbchem.a021823
bibo:pmid	9399582
has license	no-cc
sha1sum (hex)	52df5162f3752eb05cbffd70e0aed5f3c76d5235
schema:url	https://doi.org/10.1093/oxfordjournals.jbchem.a021823
resource representing a document's title	Alanyl Aminopeptidase from Human Seminal Plasma: Purification, Characterization, and Immunohistochemical Localization in the Male Genital Tract(1)
has PubMed Central identifier	PMC7110146
has PubMed identifier	9399582
schema:publication	J Biochem
resource representing a document's body	covid:52df5162f3752eb05cbffd70e0aed5f3c76d5235#body_text
is schema:about of	named entity 'homogeneity' named entity 'Leu' named entity 'substrates' named entity 'stained' named entity 'Characterization' named entity 'Male' named entity 'RELEASED' named entity 'LYS-' named entity 'PRO-SER' named entity 'COINCIDENT' named entity 'GLY-' named entity 'FINDINGS' named entity 'ELASTASE' named entity 'MOLECULAR WEIGHT' named entity 'LIKE' named entity 'EPITHELIAL CELLS' named entity 'ORDER' named entity 'ASN-PRO-ALA' named entity 'SITE' named entity 'NATIVE' named entity 'SDS-PAGE' named entity 'PROSTATE' covid:arg/52df5162f3752eb05cbffd70e0aed5f3c76d5235 named entity 'membrane' named entity 'plasma' named entity 'enzyme' named entity 'structure' named entity 'presence' named entity 'age' named entity 'sequenced' named entity 'prostate' named entity 'cDNA' named entity 'aminopeptidase' named entity 'seminal' named entity 'Lys' named entity 'molecular weight' named entity 'completely' named entity 'bestatin' named entity 'sequence' named entity 'Immunohistochemical' named entity 'radial immunodiffusion' named entity 'enzyme' named entity 'CD13' named entity 'luminal' named entity 'Arg' named entity 'alanyl aminopeptidase' named entity 'cDNA' named entity 'transmembrane' named entity 'Thr' named entity 'Thr' named entity 'SDS-PAGE' named entity 'aminopeptidase' named entity 'amide' named entity 'elastase' named entity 'Thr' named entity 'amino acid sequence' named entity 'Gln' named entity 'molecular weight' named entity 'Alanyl Aminopeptidase' named entity 'FPLC' named entity 'iodoacetamide' named entity 'Immunohistochemical staining' named entity 'pmol' named entity 'peptides' named entity 'pepsin' named entity 'azoospermic' named entity '7.5' named entity 'paraffin' named entity 'IgG' named entity 'monomer' named entity 'Coomassie Brilliant Blue' named entity 'chymotrypsin' named entity 'isoelectric point' named entity 'plasma'

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