ISSN:
1573-3904
Keywords:
Cathepsin D hemoglobin hydrolysis
;
Hemorphins release
;
Photodiode array detection
;
Radioimmunoassay
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Morphinomimetic peptides have been purified fromhemoglobin enzymatic hydrolysates and a significantamount of evidence has been accumulated indicatingthat the generation of these peptides (hemorphins)might occur in vivo. In order to investigatetheir putative physiological role and processing fromhemoglobin in vivo, two methods were developed:a specific radioimmunoassay and a UV spectracomparison analysis. These methods were applied to acathepsin D bovine hemoglobin hydrolysate and allowedthe detection of two hemorphin-7 peptides. Thisobservation supports the putative implication ofcathepsin D in the in vivo release ofhemorphins. Among the two methods used in this study,the immunological approach exhibits highersensitivity and represents a useful method toinvestigate the in vivo role and physiologicalprocessing of hemorphins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008888519322
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