Purification and Characterization of a Melanoma Cell Plasminogen Activator

Wallén, Per; Pohl, Gunnar; Bergsdorf, Nils; Rånby, Mats; Ny, Tor; Jörnvall, Hans

doi:10.1111/j.1432-1033.1983.tb07418.x

Cited by 143 publications

(31 citation statements)

References 21 publications

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“…Preparations apparently exhibiting only S-chains have also been reported [4]. Plasmin (apart from giving the two-chain cleavage) cleaves off the extra N-terminal tripeptide in the L-chain [2], thus removing the N-terminal S/L heterogeneity in the A-chain. Therefore, the A-chain is always S-type.…”

Section: Introductionmentioning

confidence: 99%

“…First, direct sequence analysis revealed that the molecules consist of polypeptides starting at different positions [2]. Thus, the material A second variation is reflected by molar mass differences, possibly due to internal carbohydrate differences in the A-part, constituting type I and type II activator molecules [4,6].…”

Section: Introductionmentioning

confidence: 99%

“…Apart from the one-chain/two-chain variation, 3 other types of possible variants have been reported [2]. First, direct sequence analysis revealed that the molecules consist of polypeptides starting at different positions [2].…”

Section: Introductionmentioning

confidence: 99%

“…A shorter cDNA segment has also been cloned [5]. On treatment with plasmin, the one-chain activator is cleaved approximately in the middle [2,3] to produce 2 disulfide-connected chains (A and B, from the N-and C-terminal ends, respectively). The B-chain is homologous to the catalytic chains of plasmin, thrombin and other serine proteases [2,4,5].…”

Section: Introductionmentioning

confidence: 99%

“…Tissue plasminogen activator has been purified from culture medium of a melanoma cell line, Bowes [1,2]. It is a one-chain glycosylated polypeptide with M, -72000 [l-3], for which a 527-residue amino acid sequence has been deduced from analysis of the corresponding cDNA [4].…”

Section: Introductionmentioning

confidence: 99%

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Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity

et al. 1983

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The N‐terminal part of native one‐chain tissue plasminogen activator from melanoma cells is not homogeneous. The protein chain starts at two different postions, in all probability representing a processing difference in the N‐terminus. Both ‘long’ L‐chains and 3‐residue shorter S‐chains are present in the preparations. In addition, results compatible with a positional Ser/Gly microheterogeneity were obtained at a single position (positions L‐4 which is equal to S‐1). The N‐terminal tripeptide difference seems to be coupled to the possible microheterogeneity: L‐chains contain Ser in this position, while S‐chains appear to contain predominantly Gly.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity

et al. 1983

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Purification of human tissue‐type plasminogen activator (t‐PA) from melanoma cell culture medium by different affinity chromatographic methods

Fischer

Zacharias

Wernicke

et al. 1990

Acta Biotechnologica

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Supernatants of a mclnnorna cell line were chromatographed on five affinity supports to ev;ilu;itr and compare purification protocols for isolation of tissue-type plasminogen activator (t-Pa). t-PA was adsorbed qunntitittively from cell culture supernatants by lysine-Sepharose, concanavulin -A-Sepharose, zinc-chelate-Sepharose and monoclonal antibody-Sepharose. The major p:rrt of t-PA wits effectively adsorbed also by heparin-Sepharose. About 20 per cent of t-PA activity piesent in the culture medium however was not bound to the latter support, which indicates a heterogeneity of melanoma t-PA. The heterogeneity is not due to carbohydrate variants I and I1 since both vnriants were adsorbed and eluted from all the affinity supports invcstignted. Highly enriched t-PA preparations were obtained by sequential chromatography on two supports. t-PA isolated by monoclonal antibody affinity chromatography and subsequently purified by gel filtration was of highest purity. Other useful combinations were chromatography on concanavalin A-Sephnrose or lysine-Sepharose followed by chromatography on heparin-Sepharose, or zinc-chelate-Seph;irose followed hy chromatography on lysine-Sepharose.

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Molecular biology of plasminogen activators and recombinant DNA progress

Cederholm-Williams

1984

BioEssays

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Purification and Characterization of a Melanoma Cell Plasminogen Activator

Cited by 143 publications

References 21 publications

Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity

Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity

Purification of human tissue‐type plasminogen activator (t‐PA) from melanoma cell culture medium by different affinity chromatographic methods

Molecular biology of plasminogen activators and recombinant DNA progress

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