Disease relevance of LOC510039

• In vitro hemolysis tests were performed under cardiopulmonary bypass (CPB; 5 L/min, 350 mmHg) and left ventricular assist device (LVAD; 5 L/min, 100 mmHg) conditions using the pivot bearing supported Gyro centrifugal pump (C1E3) [1].
• CONCLUSION: It is suggested that a portable pulsatile ECLS like T-PLS may be used as a CPB device and as an alternative CPR (cardiopulmonary resuscitation) device in the case of cardiac arrest [2].
• Serum carboxypeptidase B levels were measured in adult cows suffering from both acute and mild babesiosis caused by Babesia divergens [3].

High impact information on LOC510039

• The beta-cell localization of human pancreatic kallikrein, an endopeptidase that, in concert with carboxypeptidase B, converts bovine proinsulin to a polypeptide with the electrophoretic mobility of insulin, suggests that pancreatic kallikrein may be involved in the physiologic activation of proinsulin [4].
• Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules [5].
• Digestion with trypsin and carboxypeptidase B yields [Met]enkephalin and [Leu]enkephalin in a ratio of almost 7 to 1 [6].
• Studies using pure enzymes showed that bovine carboxypeptidase A hydrolyzed the cholyl conjugates of the neutral L-alpha-amino acids with similar specificity as observed for the human pancreatic juice, whereas bovine carboxypeptidase B cleaved the basic amino acid conjugates [7].
• This pattern of selectivity might be attributable to a limited homology of a 11-amino acid sequence with sequences within the activation segments of CPA and CPB known to interact with residues within their active sites [8].

Biological context of LOC510039

• Amino-acid sequence of bovine carboxypeptidase B [9].
• Detailed characterization of three overlapping rat genomic clones demonstrated that the coding region for the rat CPB precursor is sequestered in 11 exons which are dispersed throughout 34 kilobase pairs of genomic DNA [10].
• Conserved sequences in the 5' flanking regions of the rat CPA1, CPA2, CPB, and other pancreas-specific genes have been identified [10].
• This shortened version of human MGP is consistent with the proposed model for COOH-terminal processing, since the amino acid substitution in the COOH terminus of the human protein, Lys79 for Gln79, would allow removal of the additional basic residues from the human MGP COOH terminus by the action of the carboxypeptidase B-like enzymic activity [11].
• Mixed studies with the alkylating reagents bromoacetyl-D-arginine and bromoacetamidobutylguanidine established their efficiency in protecting the active-center glutamic acid and tyrosine of bovine carboxypeptidase B, respectively, from irreversible alkylation [12].

Anatomical context of LOC510039

• The amino-acid sequence of bovine carboxypeptidase B [peptidyl-L-lysine(-L-arginine)hydrolase, EC 3.4.12.3] has been determined using the heavy and light chains of the enzyme isolated from spontaneously activated pancreatic juice [9].
• Peptides of up to 25,000 daltons that express opiate activity only following digestion with enzymes, such s trypsin and carboxypeptidase B, also are secreted from chromaffin cells in the same proportion of their cellular content as are catecholamines and opioid peptides [13].
• Accordingly, C5a, purified from zymosan-activated human, and C5a des Arg, prepared by incubating C5a with immobilized porcine carboxypeptidase B, were studied for fibroblast chemotactic activity [14].
• Purification of carboxypeptidase B from human pancreas [15].
• A carboxypeptidase B-like enzyme was detected in the soluble fraction of purified insulin secretory granules, and implicated in insulin biosynthesis [16].

Associations of LOC510039 with chemical compounds

• The exception is the replacement of Ile-255 at the bottom of the substrate binding pocket of carboxypeptidase A, by aspartic acid in carboxypeptidase B. This single change can account for the difference in specificity of the two enzymes [9].
• The carboxypeptidase B which converts the oxytocinyl peptides showed a fairly sharp pH dependence with an optimum of 5.5-6, was activated by cobalt ion, and was inhibited by cupric ion, EDTA, and a thiol protease inhibitor, p-chloromercuribenzoate [17].
• It had biochemical and catalytic characteristics similar to those of lysosomal carboxypeptidase B. When leupeptin, an inhibitor of lysosomal carboxypeptidase B, was included in the buffers used for the preparation of PA28, PA28 activity was detected in tissues which otherwise failed to demonstrate this activity [18].
• Fractions containing proenkephalin fragments were digested with trypsin and carboxypeptidase B to liberate Met-enkephalin sequences and subjected to a second HPLC step to demonstrate association of radiolabel with Met-enkephalin [19].
• In this investigation Sephacryl-300 gel filtration chromatography of guinea pig striata, extracted in 8 M urea, demonstrated several peaks of both bioactive and immunoreactive enkephalin-like peptides after enzymatic digest (trypsin followed by carboxypeptidase B) [20].

Other interactions of LOC510039

• A plausible sequence of proteolytic cleavages that could generate the 79-residue form of MGP would be a trypsin-like cleavage at Arg80-Arg81 or Arg81-Gly82 followed by carboxypeptidase B-like cleavage to remove COOH-terminal arginine(s) [11].
• Digestion of this peptide with aminopeptidase M and carboxypeptidase B yielded a tetrapeptide (residues 6 through 9) [21].
• Serum acetylcholinesterase possesses trypsin-like and carboxypeptidase B-like activity [22].

Analytical, diagnostic and therapeutic context of LOC510039

• Proteins obtained by translation of bovine adrenal medullary mRNA in the presence of [35S]methionine were digested with trypsin and carboxypeptidase B. The resultant peptides were immunoprecipitated with anti[Met]enkephalin serum and subsequently analyzed by reverse phase HPLC [23].
• The carboxypeptidase B was separated from a less specific carboxypeptidase present in granule lysate by gel filtration on Sephacryl S-300 [17].
• The presence of [35S]Met-enkephalin sequences in this protein was confirmed by high pressure liquid chromatography of trypsin/carboxypeptidase B digests [24].
• Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma [25].
• Percoll density gradient centrifugation (after preliminary differential centrifugation) also yielded granule fractions enriched in the specific carboxypeptidase B activity [17].

References