5GHK

Crystal Structure Analysis of Canine serum albumin

Summary for 5GHK

• Entry DOI: 10.2210/pdb5ghk/pdb
• Descriptor: Serum albumin (1 entity in total)
• Functional Keywords: plasma protein, transport protein
• Biological source: Canis lupus familiaris (Dog)
• Total number of polymer chains: 1
• Total formula weight: 65801.04

Authors

Kihira, K.,Yamada, K.,Kureishi, M.,Yokomaku, K.,Shinohara, R.,Akiyama, M.,Komatsu, T. (deposition date: 2016-06-20, release date: 2016-11-23, Last modification date: 2024-10-16)

Primary citation

Yamada, K.,Yokomaku, K.,Kureishi, M.,Akiyama, M.,Kihira, K.,Komatsu, T.
Artificial Blood for Dogs
Sci Rep, 6:36782-36782, 2016

PubMed Abstract: There is no blood bank for pet animals. Consequently, veterinarians themselves must obtain "blood" for transfusion therapy. Among the blood components, serum albumin and red blood cells (RBCs) are particularly important to save lives. This paper reports the synthesis, structure, and properties of artificial blood for the exclusive use of dogs. First, recombinant canine serum albumin (rCSA) was produced using genetic engineering with Pichia yeast. The proteins showed identical features to those of the native CSA derived from canine plasma. Furthermore, we ascertained the crystal structure of rCSA at 3.2 Å resolution. Pure rCSA can be used widely for numerous clinical and pharmaceutical applications. Second, hemoglobin wrapped covalently with rCSA, hemoglobin-albumin cluster (Hb-rCSA), was synthesized as an artificial O-carrier for the RBC substitute. This cluster possesses satisfactorily negative surface net charge (pI = 4.7), which supports enfolding of the Hb core by rCSA shells. The anti-CSA antibody recognized the rCSA exterior quantitatively. The O-binding affinity was high (P = 9 Torr) compared to that of the native Hb. The Hb-rCSA cluster is anticipated for use as an alternative material for RBC transfusion, and as an O therapeutic reagent that can be exploited in various veterinary medicine situations.

PubMed: 27830776
DOI: 10.1038/srep36782

Experimental method

X-RAY DIFFRACTION (3.2 Å)