Edman Degradation

2019 ◽  
Author(s):  
Ján Labuda ◽  
Richard P. Bowater ◽  
Miroslav Fojta ◽  
Günter Gauglitz ◽  
Zdeněk Glatz ◽  
...  
Keyword(s):  
Edman Degradation

Sequencing of peptoid peptidomimetics by Edman degradation

1998 ◽  
Vol 39 (21) ◽  
pp. 3589-3592 ◽  
Author(s):  
Astrid Boeijen ◽  
Rob M.J. Liskamp
Keyword(s):  
Edman Degradation

scholarly journals Crotalase, a Fibrinogen-Clotting Snake Venom Enzyme: Primary Structure and Evidence for a Fibrinogen Recognition Exosite Different from Thrombin

1999 ◽  
Vol 81 (01) ◽  
pp. 81-86 ◽  
Author(s):  
Agnes Henschen-Edman ◽  
Ida Theodor ◽  
Brian Edwards ◽  
Hubert Pirkle
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Spatial Modeling ◽  
Glycosylation Site ◽  
Amino Sugars ◽  
Edman Degradation ◽  
Heparin Binding ◽  
Heparin Binding Site ◽  
Total Molecular Weight

SummaryCrotalase, a fibrinogen-clotting enzyme isolated from the venom of Crotalus adamanteus, and its overlapping fragments were subjected to Edman degradation. The resulting amino acid sequence, VIGGDEC NINEHRFLVALYDYWSQLFLCGGTLINNEWVLTAAHCDRTHI LIYVGVHDRSVQFDKEQRRFPKEKYFFDCSNNFTKWDKDIM LIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRAMGWGQTTSPQET LPDVPHCANINLLDYEVCRTAHPQFRLPATSRTLCAGVLEG GIDTCNRDSGGPLICNGQFQGIVFWGPDPCAQPDKPGLYTK VFDHLDWIQSIIAGEKTVNCP, is characteristic of a serine protein-ase. Comparison with thrombin, the physiological fibrinogen-clotting enzyme, showed that thrombin’s fibrinogen-recognition exosite (FRE) is poorly represented in crotalase. Hirudin, a FRE-dependent inhibitor, had no effect on crotalase. Spatial modeling of crotalase yielded a possible alternative fibrinogen-recognition site comprised of Arg 60F, Lys 85, Lys 87, and Arg 107 (underlined in the sequence above). Crotalase also lacks thrombin’s YPPW loop, as well as its functionally important ETW 146-148, and its heparin-binding site. The enzyme contains a single asparagine-linked glycosylation site, NFT, bearing neutral and amino sugars that account for 8.3% of the enzyme’s total molecular weight of 29,027. The calculated absorbance of crotalase at 280 nm, 1%, cm-1is 15.2.

scholarly journals A photothermally responsive nanoprobe for bioimaging based on Edman degradation

Nanoscale ◽  
2016 ◽  
Vol 8 (20) ◽  
pp. 10553-10557 ◽  
Author(s):  
Yi Liu ◽  
Zhantong Wang ◽  
Huimin Zhang ◽  
Lixin Lang ◽  
Ying Ma ◽  
...  
Keyword(s):  
Edman Degradation ◽  
New Type

A new type of photothermally responsive nanoprobe based on Edman degradation has been synthesized and characterized.

Characterisation of individual N-and O-linked glycosylation sites using Edman degradation

1995 ◽  
pp. 83-90 ◽  
Author(s):  
A.A. Gooley ◽  
N.H. Packer ◽  
A. Pisano ◽  
J.W. Redmond ◽  
K.L. Williams ◽  
...  
Keyword(s):  
Edman Degradation ◽  
Glycosylation Sites

scholarly journals Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

2020 ◽  
Vol 21 (12) ◽  
pp. 4383
Author(s):  
Katherine Falkowski ◽  
Ewa Bielecka ◽  
Ida B. Thøgersen ◽  
Oliwia Bocheńska ◽  
Karolina Płaza ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Gelatin Zymography ◽  
Amino Acid Sequences ◽  
Initial Assessment ◽  
Edman Degradation ◽  
Activation Domain ◽  
Additional Layer ◽  
Murine Fibroblasts ◽  
Membrane Type

Kallikrein-related peptidases (KLKs) and matrix metalloproteinases (MMPs) are secretory proteinases known to proteolytically process components of the extracellular matrix, modulating the pericellular environment in physiology and in pathologies. The interconnection between these families remains elusive. To assess the cross-activation of these families, we developed a peptide, fusion protein-based exposition system (Cleavage of exposed amino acid sequences, CleavEx) aiming at investigating the potential of KLK14 to recognize and hydrolyze proMMP sequences. Initial assessment identified ten MMP activation domain sequences which were validated by Edman degradation. The analysis revealed that membrane-type MMPs (MT-MMPs) are targeted by KLK14 for activation. Correspondingly, proMMP14-17 were investigated in vitro and found to be effectively processed by KLK14. Again, the expected neo-N-termini of the activated MT-MMPs was confirmed by Edman degradation. The effectiveness of proMMP activation was analyzed by gelatin zymography, confirming the release of fully active, mature MT-MMPs upon KLK14 treatment. Lastly, MMP14 was shown to be processed on the cell surface by KLK14 using murine fibroblasts overexpressing human MMP14. Herein, we propose KLK14-mediated selective activation of cell-membrane located MT-MMPs as an additional layer of their regulation. As both, KLKs and MT-MMPs, are implicated in cancer, their cross-activation may constitute an important factor in tumor progression and metastasis.

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