Owen M C, Ockelford P A, Wells R M
Department of Clinical Biochemistry, Christchurch Hospital, New Zealand.
Hemoglobin. 1993 Dec;17(6):513-21. doi: 10.3109/03630269309043491.
Hb Howick or beta 37(C3) Trp-->Gly is a newly described hemoglobin variant found in an adult male. Hematological data and stability by the isopropanol stability test were normal. The abnormal variant comprised 29% of total hemoglobin and migrated in the Hb D position on cellulose acetate at pH 8.6, and in the Hb F position on citrate agar (pH 6.0). Oxygen dissociation studies on the whole blood showed the variant to have a higher oxygen affinity than normal, with a P50 of 19.8 mm Hg (normal, 26 mm Hg). There were also significant differences in the saturation curve. The variant showed a reduced Bohr effect which was manifested as very high oxygen affinity at low pH and saturation. The beta 37 residue is an alpha 1 beta 2 contact site and the substitution of the tryptophan for a glycine would be expected to result in a destabilization of the deoxy-hemoglobin form because of the reduced number of hydrogen bonds, salt bridges and van der Waal contacts between the alpha 1 and beta 2 chains.
血红蛋白豪伊克（Hb Howick）或β37（C3）色氨酸（Trp）突变为甘氨酸（Gly）是在一名成年男性中发现的一种新描述的血红蛋白变体。通过异丙醇稳定性试验得出的血液学数据和稳定性均正常。异常变体占总血红蛋白的29%，在pH 8.6的醋酸纤维素上迁移至血红蛋白D位置，在pH 6.0的柠檬酸盐琼脂上迁移至血红蛋白F位置。对全血进行的氧解离研究表明，该变体的氧亲和力高于正常水平，P50为19.8毫米汞柱（正常为26毫米汞柱）。饱和曲线也存在显著差异。该变体的玻尔效应降低，表现为在低pH值和饱和度下具有非常高的氧亲和力。β37残基是α1β2接触位点，色氨酸被甘氨酸取代预计会导致脱氧血红蛋白形式不稳定，因为α1和β2链之间的氢键、盐桥和范德华接触数量减少。
