Scientific corner

Observation of Granulocyte Adsorption in Adacolumn® Cellulose Acetate Beads after Granulocytapheresis.

Toshiyuki Okuno 1 2Yutaka Yoshida 1Yuriko Takaki 1Yasuyuki Araki 1Hironobu Inoue 3Kazuaki Soejima 1 3Yuki Okado 4Kenichi Yoshida 4Haruo Imamura 4Satoshi Hagiwara 5Shigekiyo Matsumoto 6Takaaki Kitano 6 , Ther Apher Dial. 2019 Jun;23(3):210-216.

Our findings suggest that granulocytes contact and adhere to each other at the surface layer after adsorption, and that granulocyte-granulocyte adhesion is enhanced by a higher inflammatory response.

https://pubmed.ncbi.nlm.nih.gov/31025504/

Scientific corner

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films

Ziwei Huang 1Vikram Singh Raghuwanshi 1Gil Garnier 1Front Bioeng Biotechnol. 2017 Jul 17:5:41. doi: 10.3389/fbioe.2017.00041

The functionality and aging mechanism of antibodies physisorbed onto cellulosic films was investigated. Blood grouping antibodies immunoglobulin G (IgG) and immunoglobulin M (IgM) were adsorbed onto smooth cellulose acetate (CAF) and regenerated cellulose (RCF) films. Cellulose films and adsorbed IgG layers were characterized at the air and liquid interface by X-ray and neutron reflectivity (NR), respectively. Cellulose film 208 Å thick (in air) swell to 386 Å once equilibrated in water. IgG adsorbs from solution onto cellulose as a partial layer 62 Å thick. IgG and IgM antibodies were adsorbed onto cellulose and cellulose acetate films, air dried, and aged at room temperature for periods up to 20 days. Antibody functionality and surface hydrophobicity were measured everyday with the size of red blood cell (RBC) agglutinates (using RBC specific to IgG/IgM) and the water droplet contact angle, respectively. The functionality of the aged IgG/IgM decreases faster if physisorbed on cellulose than on cellulose acetate and correlates to surface hydrophobicity. IgG physisorbed on RCF or CAF age better and remain functional longer than physisorbed IgM. We found a correlation between antibody stability and hydrogen bond formation ability of the system, evaluated from antibody carbonyl concentration and cellulosic surface hydroxyl concentration. Antibody physisorbs on cellulose by weak dipole forces and hydrogen bonds. Strong hydrogen bonding contributes to the physisorption of antibody on cellulose into a non-functional configuration in which the molecule relaxes by rotation of hydophobic groups toward the air interface.

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PubMed (nih.gov)

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PMC (nih.gov)

Scientific corner

Advancements in Inflammatory Bowel Disease: A Narrative Review of Diagnostics, Management, Epidemiology, Prevalence, Patient Outcomes, Quality of Life, and Clinical Presentation

Muhammad Ali Muzammil 1Fnu Fariha 2Tirath Patel 3Rohab Sohail 4Munesh Kumar 5Ejaz Khan 6Bushra Khanam 7Satesh Kumar 8Mahima Khatri 9Giustino Varrassi 10Prasanthi Vanga 112023 Jun 28;15(6):e41120. doi: 10.7759/cureus.41120.

The functionality and aging mechanism of antibodies physisorbed onto cellulosic films
was investigated. Blood grouping antibodies immunoglobulin G (IgG) and immunoglobulin M (IgM) were adsorbed onto smooth cellulose acetate (CAF) and regenerated
cellulose (RCF) films. Cellulose films and adsorbed IgG layers were characterized at the
air and liquid interface by X-ray and neutron reflectivity (NR), respectively. Cellulose film
208 Å thick (in air) swell to 386 Å once equilibrated in water. IgG adsorbs from solution
onto cellulose as a partial layer 62 Å thick. IgG and IgM antibodies were adsorbed onto
cellulose and cellulose acetate films, air dried, and aged at room temperature for periods
up to 20 days. Antibody functionality and surface hydrophobicity were measured everyday with the size of red blood cell (RBC) agglutinates (using RBC specific to IgG/IgM)
and the water droplet contact angle, respectively. The functionality of the aged IgG/IgM
decreases faster if physisorbed on cellulose than on cellulose acetate and correlates to
surface hydrophobicity. IgG physisorbed on RCF or CAF age better and remain functional longer than physisorbed IgM. We found a correlation between antibody stability
and hydrogen bond formation ability of the system, evaluated from antibody carbonyl
concentration and cellulosic surface hydroxyl concentration. Antibody physisorbs on cellulose by weak dipole forces and hydrogen bonds. Strong hydrogen bonding contributes
to the physisorption of antibody on cellulose into a non-functional configuration in which
the molecule relaxes by rotation of hydophobic groups toward the air interface.

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PubMed (nih.gov)

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