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Fibrin polymerization, an important component of blood clotting, involves the conversion of soluble fibrinogen molecules in the blood plasma to fibrin monomers. These monomers can then polymerize to form a gel that is a major structural component of a blood clot. Oligomers composed of both fibrinogen and fibrin can form and are thought to impact the kinetics of the fibrin gelation process. Fibrinogen plays a dual role in fibrin polymerization; it can occupy available binding sites by binding to fibrin, inhibiting gelation, and it can be converted to fibrin in monomeric or oligomeric form to facilitate gel formation. Here, we present two kinetic polymerization models with gelation that are used to study the effects of fibrin-fibrinogen interactions on fibrin polymerization. These models can help characterize the conditions under which a gel forms and examine how fibrinogen-fibrin binding and fibrinogen conversion impacts the gel structure, if one forms.