Studies on Thrombolysis with Streptokinase

Summary1. Human thrombi of various ages obtained by surgery were incubated in SK solution. Whereas thrombi up to 2 days old showed no considerable lysis, older thrombi, in some cases more than 1 month old, showed good lysibility in SK.2. The good lysibility of older thrombi was reproduced in in vitro whole blood clots.3. Similar to the findings obtained in experimental thrombi, we found that in in vitro whole blood clots retraction goes along with a marked decrease in the water content, whereas we find again a moderate rise with increasing age.4. If we add 131I-labelled human serum albumin to the supernatant of in-vitro clots, we see an increased absorption of albumin, particularly in the second and third day after clotting.5. Massive hemolysis sets in on the second and third day in whole blood clots incubated at 37 centigrades in their own serum.6. The following are discussed as possible causes for the improved lysibility of older thrombi and clots : renewed absorption of plasminogen from the milieu ; the release of ferments that may be activated by SK in the process of cytolysis, and a decrease in the content of plasmin inhibitors.7. Based on the findings the suggestion is advanced to attempt lytic therapy with SK even in the case of older clinical thrombi.

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Study on the interaction of ertugliflozin with human serum albumin in vitro by multispectroscopic methods, molecular docking, and molecular dynamics simulation

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2019.04.047 ◽

2019 ◽

Vol 219 ◽

pp. 83-90 ◽

Cited By ~ 14

Author(s):

Wenjing Wang ◽

Na Gan ◽

Qiaomei Sun ◽

Di Wu ◽

Ruixue Gan ◽

...

Keyword(s):

Molecular Dynamics ◽

Molecular Docking ◽

Molecular Dynamics Simulation ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Dynamics Simulation

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Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

Journal of Molecular Liquids ◽

10.1016/j.molliq.2021.116888 ◽

2021 ◽

pp. 116888

Author(s):

Fahad A. Alhumaydhi ◽

Mohammad Abdullah Aljasir ◽

Abdullah S.M. Aljohani ◽

Suliman A. Alsagaby ◽

Ameen S.S. Alwashmi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

In Silico

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Synthesis and In Vitro Assessment of pH-Sensitive Human Serum Albumin Conjugates of Pirarubicin

Pharmaceuticals ◽

10.3390/ph14010022 ◽

2020 ◽

Vol 14 (1) ◽

pp. 22

Author(s):

Kenji Tsukigawa ◽

Shuhei Imoto ◽

Keishi Yamasaki ◽

Koji Nishi ◽

Toshihiko Tsutsumi ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Coupling Reaction ◽

Synthetic Polymer ◽

Ph Sensitive ◽

Acidic Ph ◽

Polymer Conjugate ◽

Acidic Conditions

In a previous study, we reported on the development of a synthetic polymer conjugate of pirarubicin (THP) that was formed via an acid-labile hydrazone bond between the polymer and the THP. However, the synthetic polymer itself was non-biodegradable, which could lead to unexpected adverse effects. Human serum albumin (HSA), which has a high biocompatibility and good biodegradability, is also a potent carrier for delivering antitumor drugs. The objective of this study was to develop pH-sensitive HSA conjugates of THP (HSA-THP), and investigate the release of THP and the cytotoxicity under acidic conditions in vitro for further clinical development. HSA-THP was synthesized by conjugating maleimide hydrazone derivatives of THP with poly-thiolated HSA using 2-iminothiolane, via a thiol-maleimide coupling reaction. We synthesized two types of HSA-THP that contained different amounts of THP (HSA-THP2 and HSA-THP4). Free THP was released from both of the HSA conjugates more rapidly at an acidic pH, and the rates of release for HSA-THP2 and HSA-THP4 were similar. Moreover, both HSA-THPs exhibited a higher cytotoxicity at acidic pH than at neutral pH, which is consistent with the effective liberation of free THP under acidic conditions. These findings suggest that these types of HSA-THPs are promising candidates for further development.

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The in Vitro Anti-HIV Efficacy of Negatively Charged Human Serum Albumin Is Antagonized by Heparin

AIDS Research and Human Retroviruses ◽

10.1089/aid.1997.13.677 ◽

1997 ◽

Vol 13 (8) ◽

pp. 677-683 ◽

Cited By ~ 3

Author(s):

P.J. SWART ◽

C.S. SUN ◽

M.E. KUIPERS ◽

C. ASUNCION ◽

S. JOSEPHS ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Anti Hiv

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Kinetic study of the photochemical changes of (ZZ)-bilirubin IX α bound to human serum albumin. Demonstration of (EZ)-bilirubin IX α as an intermediate in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α

Biochemical Journal ◽

10.1042/bj2260251 ◽

1985 ◽

Vol 226 (1) ◽

pp. 251-258 ◽

Cited By ~ 25

Author(s):

S Itoh ◽

S Onishi

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Kinetic Study ◽

Human Serum ◽

Photochemical Reaction ◽

Relative Rate ◽

Significant Preference ◽

Geometrical Isomers ◽

Relative Rate Constants

The present study was performed to elucidate why the photochemical reaction of (ZZ)-bilirubin bound to human serum albumin is singularly selective, and only one of the two (EZ)- and (ZE)-bilirubins, the (ZE)-isomer, is produced. In a kinetic study of the photochemical reaction in vitro, the sum of the relative rate constants of photochemical transformation of (EZ)-bilirubin into both (EZ)-cyclobilirubin and (ZZ)-bilirubin, with a significant preference for the former, was proved to be considerably larger than that of the transformation of (ZZ)-bilirubin into (EZ)-bilirubin. Therefore only one of the geometrical isomers, namely (ZE)-bilirubin, is apparently formed. It was concluded that (EZ)-bilirubin photochemically undergoes (EZ)-cyclization, i.e. structural photoisomerization, while bound to its high-affinity site on human serum albumin, and is an intermediate in the transformation of (ZZ)-bilirubin into (EZ)-cyclobilirubin.

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