The differentiation of fluorescamine-modified kinins by gel electrophoresis

Prakash, Ajai; Roffman, Steven; Greenbaum, Lowell M.

doi:10.1016/0003-2697(78)90748-0

Cited by 5 publications

(2 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reason that clear separation may be obtained is the fact that fluorescamine causes differential charges on the various kinins allowing separation [ 19]. A partial sequence of Leu-Ala-Tyr-Thr-was found at the amino terminal position of leukokinin-H.…”

Section: Discussionmentioning

confidence: 99%

“…Leukokinin-H was subjected to polyacrylamide gel electrophoresis after modification by fluorescamine according to the general methods for peptides [18] as described by PRAKASH, ROFFMAN and GREENRAUM [19]. 20 /~1 of a solution of leukokinin-H containing biological activity equivalent to 1/zg/ml of bradykinin was mixed with 50/zg of 0.05 M sodium borate buffer, pH 8.1, containing 50% (v/v) glycerol and reacted with 5/zl of freshly prepared fluorescamine solution (3 mg/ml) in acetone while vigorously mixing.…”

Section: Procedures Used In Testing Leukokinin-h For Puritymentioning

confidence: 99%

See 1 more Smart Citation

Leukokinin-H generated from human ascites fluid; its isolation and pharmacology

1979

View full text Add to dashboard Cite

Leukokinin-H, a pharmacologically active peptide, has been isolated from human ascites fluid following its generation in vitro at acid pH. The peptide has a molecular weight of approximately 2500. The partial sequence of Leu-AlaTyr-Thr-was obtained from the amino-terminal end. Arginine is the terminal amino acid at the carboxyl end.It was demonstrated that while cell-free ascites fluid generates leukokinin-H, the presence of neoplastic cells enhances the formation about 5 fold. A bradykinin-llke peptide was formed in the fluid following storage at a low temperature of 4~The presence of neoplastic cells, however, did not enhance this peptide formation.Procedures are described for the isolation of leukokinln-H by chromatography. The peptide was clearly differentiated from bradykinin, Lys-bradykinin and MetLys-bradyklnin by treatment of the leukoklnin and other kinins with fluorescamine and separation of the fluorescamlne peptides bygel electrophoresls. The pharmacology of leukokiuln-H isolated" from human ascites fluid is described and compared with bradykinin and leukoklnlns PMN and M. Like the other kinins, it is a potent agent in causing vascular permeability. Likewise it is a vasodepressor substance. Unlike bradykinin it has little spasmogenlc activity on the guinea pig ileum. Its pharmacological properties as well as other evidence cited indicates that it may play an important role as a permeability factor in ascites fluid accumulation of neoplastic etiology.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Procedures Used In Testing Leukokinin-h For Puritymentioning

confidence: 99%