Glycated hemoglobin 10

There are many elements distributed in the human body. These elements have different reference standards. They are normal within the normal level range, and have a great impact on the body within the abnormal level range. First of all, glycated hemoglobin is not too serious, but it is on the high side. The patient's blood sugar is relatively poor and needs to be controlled in time.

Is Glycated Hemoglobin 10 serious?

The general reference range of glycated hemoglobin is between 4% and 6%. If the glycated hemoglobin is 10, it means that the patient's blood sugar control in the past three months is very poor.

Glycated hemoglobin reflects the average blood sugar control in the past three months. If this value is 10%, then the patient estimates that the average blood sugar level in the past three months is around fifteen to sixteen. This means that if the patient's fasting blood sugar level before a meal is seven or eight, the post-meal blood sugar level may reach more than twenty.

Therefore, the result of this glycated hemoglobin can only mean that the patient's blood sugar control has been relatively poor in the recent period, that is, in the past three months. As for its severity, it needs to be combined with other test results. For example, it is necessary to check the patient for some complications, which is also very important. Just looking at the test results of glycosylated hemoglobin can only infer the recent blood sugar control situation, but cannot simply rely on this value to determine whether the condition is serious.

Research History

Glycated hemoglobin was first separated from other types of hemoglobin using chromatography in 1958 and classified as a glycoprotein in 1968. In 1969, it was discovered that the amount of glycosylated hemoglobin was increased in patients with diabetes. In 1975, researchers obtained the reaction formula for producing glycated hemoglobin.

The terminology for the glycation products of glucose and other carbohydrates bound to hemoglobin has changed several times since the first description of the abnormal hemoglobin found in diabetic patients in 1968. Since 1986, IUPAC-IUB (International Union of Pure and Applied Chemistry) has recommended the use of the name glycated hemoglobin, ie the non-enzymatic glycosylation of hemoglobin. On the other hand, the more advanced term glycosylated hemoglobin is frequently used in everyday language and in current publications.

According to each glycation site and reaction participant, the total glycated hemoglobin is divided into several subfractions.

Native (non-glycated) hemoglobin is A0 (2α, 2β chains). Subfractions (HbA1a1, HbA1a2, HbA1b and HbA1c) are formed by glycosylation of the free amino group of the N-terminal valine of the hemoglobin β chain with different carbohydrates. These subfractions are collectively referred to as HbA1. In addition to the N-terminal valine of the hemoglobin β chain, other free amino groups in the hemoglobin molecule are also involved in glycosylation (N-terminal valine of the α chain, lysine ε-amino group).

Relative to HbA1, hemoglobin with all β-chain N-terminal glycosylation and other free amino groups is called total glycated hemoglobin. In addition to the basic adult hemoglobin AO, small amounts of fetal hemoglobin HbF (2α, 2γ chains) and hemoglobin A2 (2α, 2δ chains) are found in healthy people. Valine is located at the N-terminus of the delta chain and is glycosylated in a similar manner, for example, by covalent bonding with glucose to form HbA2c. Glycated hemoglobin measured by affinity chromatography was taken as total glycated hemoglobin.