Hydrodynamics of cryogelation

Keiichi Miyamoto; Yoshiyuki Shimonishi; Masayuki Tokita; Takashi Komai

doi:10.1016/S0141-8130(01)00168-4

Hydrodynamics of cryogelation

Keiichi Miyamoto, Yoshiyuki Shimonishi, Masayuki Tokita, Takashi Komai

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Cryogel, prevalent in the plasma of rheumatoid arthritis patients, is a plasma fibronectin (pFN)-extra domain A containing FN [EDA(+)FN]-fibrinogen (Fbg) aggregate formed by the addition of heparin (Hep) at low temperature. Although EDA(+)FN is not usually present in normal plasma, its prevalence in rheumatic patients induces cryogelation. In this study, we determined the hydrodynamic radius (R_h) ratio (R_h/R_h30) of the cryogel component by dynamic light scattering in vitro. R_h/R_h30 was normalized to R_h at 30 °C (R_h30) at several temperatures. The R_h/R_h30 of Fbg was found to increase only by self-aggregation, whereas the R_h/R_h30 of FNs does not increase in response to temperature changes. The R_h/R_h30 of the Fbg/FN aggregate is increased by the addition of Hep, and the R_h/R_h30 (12.5) of the Hep-induced EDA(+)FN/Fbg aggregate is greater than that (2.5) of the pFN/Fbg aggregate. These results suggest that cryogelation requires Fbg self-aggregation and the interaction between EDA(+)FN and Hep.

Original language	English
Pages (from-to)	219-223
Number of pages	5
Journal	International Journal of Biological Macromolecules
Volume	29
Issue number	4-5
DOIs	https://doi.org/10.1016/S0141-8130(01)00168-4
Publication status	Published - Dec 10 2001
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Molecular Biology
Economics and Econometrics
Energy(all)

Access to Document

10.1016/S0141-8130(01)00168-4

Cite this

@article{b1c9f13b744b483e90c6bdb9bbd03d46,

title = "Hydrodynamics of cryogelation",

abstract = "Cryogel, prevalent in the plasma of rheumatoid arthritis patients, is a plasma fibronectin (pFN)-extra domain A containing FN [EDA(+)FN]-fibrinogen (Fbg) aggregate formed by the addition of heparin (Hep) at low temperature. Although EDA(+)FN is not usually present in normal plasma, its prevalence in rheumatic patients induces cryogelation. In this study, we determined the hydrodynamic radius (Rh) ratio (Rh/Rh30) of the cryogel component by dynamic light scattering in vitro. Rh/Rh30 was normalized to Rh at 30 °C (Rh30) at several temperatures. The Rh/Rh30 of Fbg was found to increase only by self-aggregation, whereas the Rh/Rh30 of FNs does not increase in response to temperature changes. The Rh/Rh30 of the Fbg/FN aggregate is increased by the addition of Hep, and the Rh/Rh30 (12.5) of the Hep-induced EDA(+)FN/Fbg aggregate is greater than that (2.5) of the pFN/Fbg aggregate. These results suggest that cryogelation requires Fbg self-aggregation and the interaction between EDA(+)FN and Hep.",

author = "Keiichi Miyamoto and Yoshiyuki Shimonishi and Masayuki Tokita and Takashi Komai",

year = "2001",

month = dec,

day = "10",

doi = "10.1016/S0141-8130(01)00168-4",

language = "English",

volume = "29",

pages = "219--223",

journal = "International Journal of Biological Macromolecules",

issn = "0141-8130",

publisher = "Elsevier",

number = "4-5",

}

TY - JOUR

T1 - Hydrodynamics of cryogelation

AU - Miyamoto, Keiichi

AU - Shimonishi, Yoshiyuki

AU - Tokita, Masayuki

AU - Komai, Takashi

PY - 2001/12/10

Y1 - 2001/12/10

N2 - Cryogel, prevalent in the plasma of rheumatoid arthritis patients, is a plasma fibronectin (pFN)-extra domain A containing FN [EDA(+)FN]-fibrinogen (Fbg) aggregate formed by the addition of heparin (Hep) at low temperature. Although EDA(+)FN is not usually present in normal plasma, its prevalence in rheumatic patients induces cryogelation. In this study, we determined the hydrodynamic radius (Rh) ratio (Rh/Rh30) of the cryogel component by dynamic light scattering in vitro. Rh/Rh30 was normalized to Rh at 30 °C (Rh30) at several temperatures. The Rh/Rh30 of Fbg was found to increase only by self-aggregation, whereas the Rh/Rh30 of FNs does not increase in response to temperature changes. The Rh/Rh30 of the Fbg/FN aggregate is increased by the addition of Hep, and the Rh/Rh30 (12.5) of the Hep-induced EDA(+)FN/Fbg aggregate is greater than that (2.5) of the pFN/Fbg aggregate. These results suggest that cryogelation requires Fbg self-aggregation and the interaction between EDA(+)FN and Hep.

AB - Cryogel, prevalent in the plasma of rheumatoid arthritis patients, is a plasma fibronectin (pFN)-extra domain A containing FN [EDA(+)FN]-fibrinogen (Fbg) aggregate formed by the addition of heparin (Hep) at low temperature. Although EDA(+)FN is not usually present in normal plasma, its prevalence in rheumatic patients induces cryogelation. In this study, we determined the hydrodynamic radius (Rh) ratio (Rh/Rh30) of the cryogel component by dynamic light scattering in vitro. Rh/Rh30 was normalized to Rh at 30 °C (Rh30) at several temperatures. The Rh/Rh30 of Fbg was found to increase only by self-aggregation, whereas the Rh/Rh30 of FNs does not increase in response to temperature changes. The Rh/Rh30 of the Fbg/FN aggregate is increased by the addition of Hep, and the Rh/Rh30 (12.5) of the Hep-induced EDA(+)FN/Fbg aggregate is greater than that (2.5) of the pFN/Fbg aggregate. These results suggest that cryogelation requires Fbg self-aggregation and the interaction between EDA(+)FN and Hep.

UR - http://www.scopus.com/inward/record.url?scp=0035842072&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035842072&partnerID=8YFLogxK

U2 - 10.1016/S0141-8130(01)00168-4

DO - 10.1016/S0141-8130(01)00168-4

M3 - Article

C2 - 11718817

AN - SCOPUS:0035842072

SN - 0141-8130

VL - 29

SP - 219

EP - 223

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - 4-5

ER -

Hydrodynamics of cryogelation

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this