Proteinase K Activity Inhibitor Near Amino Acids Carrying Large Substituents: Three PAH Diolepoxides Covalently Modify His-146 Human Serum Albumin Residue

1994 ◽  
Vol 116 (16) ◽  
pp. 7407-7408 ◽  
Author(s):  
Joseph Zaia ◽  
Klaus Biemann
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Proteinase K ◽  
K Activity

In vitro stereoselective degradation of carprofen glucuronide by human serum albumin. Characterization of sites and reactive amino acids

Chirality ◽  
2000 ◽  
Vol 12 (2) ◽  
pp. 53-62 ◽  
Author(s):  
H�l�ne Georges ◽  
Nathalie Presle ◽  
Thierry Buronfosse ◽  
Sylvie Fournel-Gigleux ◽  
Patrick Netter ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Stereoselective Degradation

Exploring the Molecular Level Interaction of Human Serum Albumin with Calcium Oxalate Monohydrate Crystals

2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao
Keyword(s):  
Amino Acids ◽  
Crystal Growth ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Calcium Oxalate ◽  
Human Serum ◽  
Stone Formation ◽  
Calcium Oxalate Monohydrate ◽  
Calcium Oxalate Crystallization ◽  
In Silico Docking

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.

scholarly journals Physicochemical characterization of carbamylated human serum albumin: an in vitro study

RSC Advances ◽  
2019 ◽  
Vol 9 (63) ◽  
pp. 36508-36516
Author(s):  
Asim Badar ◽  
Zarina Arif ◽  
Shireen Naaz Islam ◽  
Khursheed Alam
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Physicochemical Characterization ◽  
In Vitro Study ◽  
Terminal Amino ◽  
Carbamyl Amino Acids

Carbamylation is an ubiquitous process in which cyanate (OCN−) reacts with the N-terminal amino or ε-amino moiety and generates α-carbamyl amino acids and ε-carbamyl-lysine (homocitrulline).

scholarly journals Tuning the interactions of decavanadate with thaumatin, lysozyme, proteinase K and human serum proteins by its coordination to a pentaaquacobalt(ii) complex cation

2019 ◽  
Vol 43 (45) ◽  
pp. 17863-17871 ◽  
Author(s):  
Lukáš Krivosudský ◽  
Alexander Roller ◽  
Annette Rompel
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Proteins ◽  
Complex Cation ◽  
Proteinase K ◽  
Human Serum Proteins

Inorganic functionalization of the decavanadate anion promotes a different type of interaction with model proteins thaumatin, lysozyme, proteinase K, human serum albumin and transferrin.

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