CASE REPORTSDouble heterozygous mutations Gln100Leu and His348Gln of the F7 gene in a patient with factor VII deficiencyLi, Mina; Zheng, Fangxiub; Jin, Yanhuib; Wang, Mingshanb; Zhu, Liqingb; Yang, LihongbAuthor Information aSchool of Laboratory Medicine, Wenzhou Medical College bDepartment of Clinical Laboratory, The First Affiliated Hospital of Wenzhou Medical College, Lucheng district, Wenzhou, China Correspondence to Mingshan Wang, Department of Clinical Laboratory, The First Affiliated Hospital of Wenzhou Medical College, 96 Fuxue Lane, Lucheng district, Wenzhou 325000, China Tel: +8657788069594; fax: +8657788069596; e-mail: firstname.lastname@example.org Received 12 March, 2012 Revised 11 April, 2012 Accepted 20 April, 2012 Blood Coagulation & Fibrinolysis: March 2013 - Volume 24 - Issue 2 - p 199-201 doi: 10.1097/MBC.0b013e3283551132 Buy Metrics Abstract A 25-year-old Chinese woman who had a history of easy bruising was admitted to hospital due to uncontrolled epistaxis. She showed factor VII activity level of 2% and factor VII antigen level of 4% of the normal value. We detected a novel missense mutation g.8355 A>T (p.Gln100Leu) in the second epidermal growth factor-like (EGF) domain and a g.11482 T>G (p.His348Gln) in the catalytic domain. Although the Gln100 residue is close to the junction of EGF-2 domain with the serine protease domain, we infer that the substitution of polar negatively charged Gln residue at the position 100 with introduction of nonpolar Leu residue may be likely to perturb proper folding, resulting in decreasing factor VII activity. © 2013 Lippincott Williams & Wilkins, Inc.